Karp’s Cell and Molecular Biology.

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Karp’s Cell and Molecular Biology

Concepts and Experiments

Ninth Edition

JANET IWASA
University of Utah

WALLACE MARSHALL
University of California, San Francisco
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COVER PHOTO CREDIT Janet Iwasa and the Innovative Genomics Institute
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EPUB ISBN: 978-1-119-59816-9
Library of Congress Cataloging-in-Publication Data
Names: Iwasa, Janet, author. | Marshall, Wallace F., author. | Karp, Gerald. Cell and molecular biology.
Title: Karp’s cell and molecular biology / Janet Iwasa, University of Utah, Wallace Marshall, University of
California, San Francisco.
Other titles: Cell and molecular biology
Description: Ninth edition. | Hoboken : Wiley, 2020. | Includes index.
Identifiers: LCCN 2019047994 (print) | LCCN 2019047995 (ebook) | ISBN
9781119598244 (paperback) | ISBN 9781119598169 (epub)
Subjects: LCSH: Cytology. | Molecular biology.
Classification: LCC QH581.2.K369 2020 (print) | LCC QH581.2 (ebook) |
DDC 571.6—dc23
LC record available at https://lccn.loc.gov/2019047994
LC ebook record available at https://lccn.loc.gov/2019047995
About the Authors

JANET IWASA is an Assistant Professor in the Biochemistry Department at the University

of Utah. She received her bachelor’s degree from Williams College and a Ph.D. in Cell Biology
from the University of California, San Francisco, where she first became interested in the
visualization of biological processes. As a postdoctoral fellow, she was awarded a fellowship
from the National Science Foundation to create a multimedia exhibit with Nobel Laureate
Jack Szostak (Harvard University) and the Museum of Science, Boston. She later joined
Harvard Medical School as a faculty member in the Department of Cell Biology, where she
utilized visualization tools to aid in scientific communication, exploration, and outreach.
Janet’s award-winning illustrations and animations have appeared in scientific journals
including Nature, Science, and Cell, as well as in the New York Times.
She currently runs a group, called the Animation Lab, that focuses on the innovative use of
visualization tools for molecular biology research, education and outreach.

WALLACE MARSHALL is Professor of Biochemistry and Biophysics at the University of

California San Francisco and an ASCB Fellow. A native Long-Islander, he received his
bachelor’s degrees in Electrical Engineering and Biochemistry from the State University of
New York at Stony Brook, and his Ph.D. in Biochemistry from UC San Francisco, where he
studied organization of chromosomes within the nucleus with John Sedat. He then moved to
Yale University for postdoctoral studies with Joel Rosenbaum, where he became interested in
questions of organelle size control and cell organization, using cilia, flagella, and centrioles as
model systems. In 2003, he joined the faculty at UCSF where he continues to study questions
of cellular organization in a variety of model organisms including green algae, yeast, ciliates,
and mammalian cells. In addition to his cell biology research, he teaches Human Metabolism
for the UCSF School of Pharmacy, Cell Biology for the UCSF Graduate Division, and a two-
week lab course on cell behavior. In 2014, he served as Program Committee Chair organizing
the annual meeting of the American Society for Cell Biology. From 2014 to 2018 he served as
co-director of the Physiology summer course at the Marine Biological Laboratory in Woods
Hole, Massachusetts. He currently directs the Center for Cellular Construction, a National
Science Foundation Science and Technology Center devoted to engineering cells.
Both authors are Council members of the American Society for Cell Biology.
Contents
Cover
Title Page
Copyright
About the Authors
Preface to the Ninth Edition
Acknowledgments
We also wish to thank all reviewers of this and previous editions
Nobel Prizes Awarded for Research in Cell and Molecular Biology Since 1958
Topics of Human Interest
CHAPTER 1: Introduction to the Study of Cell and Molecular Biology
1.1 The Discovery of Cells
1.2 Basic Properties of Cells
1.3 Two Fundamentally Different Classes of Cells
1.4 Viruses and Viroids
1.5 Green Cells: Volvox, an Experiment in Multicellularity
1.6 Engineering Linkage: Tissue Engineering
Analytic Questions
CHAPTER 2: The Chemical Basis of Life
2.1 Covalent Bonds
2.2 Engineering Linkage: Radionuclides for Imaging and Treatment
2.3 Noncovalent Bonds
2.4 Acids, Bases, and Buffers
2.5 The Nature of Biological Molecules
2.6 Green Cells: Chemical Fertilizers
2.7 Four Types of Biological Molecules
2.8 The Formation of Complex Macromolecular Structures
Analytic Questions
CHAPTER 3: Bioenergetics, Enzymes, and Metabolism
3.1 Bioenergetics
3.2 Enzymes as Biological Catalysts
3.3 Metabolism
3.4 Green Cells: Regulation of Metabolism by the Light/Dark Cycle
3.5 Engineering Linkage: Using Metabolism to Image Tumors
Analytic Questions
CHAPTER 4: The Structure and Function of the Plasma Membrane
4.1 Introduction to the Plasma Membrane
 4.2 The Chemical Composition of Membranes
4.3 Membrane Proteins
4.4 Membrane Lipids and Membrane Fluidity
4.5 The Dynamic Nature of the Plasma Membrane
4.6 The Movement of Substances across Cell Membranes
4.7 Membrane Potentials and Nerve Impulses
4.8 Green Cells: Electrical Signaling in Plants
4.9 Engineering Linkage: Neurotechnology
Analytic Questions
CHAPTER 5: Aerobic Respiration and the Mitochondrion
5.1 Mitochondrial Structure and Function
5.2 Aerobic Metabolism in the Mitochondrion
5.3 The Role of Mitochondria in the Formation of ATP
5.4 Engineering Linkage: Measuring Blood Oxygen
5.5 Establishment of a Proton-Motive Force
5.6 The Machinery for ATP Formation
5.7 Peroxisomes
5.8 Green Cells: Glyoxysomes
Analytic Questions
CHAPTER 6: Photosynthesis and the Chloroplast
6.1 The Origin of Photosynthesis
6.2 Chloroplast Structure
6.3 An Overview of Photosynthetic Metabolism
6.4 The Absorption of Light
6.5 Green Cells: Chromoplasts
6.6 Photosynthetic Units and Reaction Centers
6.7 Photophosphorylation
6.8 Carbon Dioxide Fixation and the Synthesis of Carbohydrate
6.9 Engineering Linkage: Photodynamic Therapy
Analytic Questions
CHAPTER 7: Interactions Between Cells and Their Environment
7.1 Extracellular Interactions
7.2 Engineering Linkage: Organoids
7.3 Interactions of Cells with Extracellular Materials
7.4 Interactions of Cells with Other Cells
7.5 Tight Junctions: Sealing the Extracellular Space
7.6 Intercellular Communication
7.7 Cell Walls
 7.8 Green Cells: Cell Walls and Plant Terrestrialization
Analytic Questions
CHAPTER 8: Cytoplasmic Membrane Systems: Structure, Function, and Membrane
Traff...
8.1 An Overview of the Endomembrane System
8.2 A Few Approaches to the Study of Endomembranes
8.3 The Endoplasmic Reticulum
8.4 The Golgi Complex
8.5 Types of Vesicle Transport
8.6 Engineering Linkage: Extracellular Vesicles for Drug Delivery
8.7 Lysosomes
8.8 Green Cells: Plant Cell Vacuoles
8.9 The Endocytic Pathway: Moving Membrane and Materials into the Cell Interior
8.10 Posttranslational Uptake of Proteins by Peroxisomes, Mitochondria, and Chlo...
Analytic Questions
CHAPTER 9: The Cytoskeleton and Cell Motility
9.1 Overview of the Major Functions of the Cytoskeleton
9.2 Structure and Function of Microtubules
9.3 Green Cells: Why the Woodbine Twineth
9.4 Motor Proteins: Kinesins and Dyneins
9.5 Microtubule-Organizing Centers (MTOCs)
9.6 Structure and Function of Cilia and Flagella
9.7 Intermediate Filaments
9.8 Actin and Myosin
9.9 Muscle Organization and Contraction
9.10 Engineering Linkage: Muscle Biomechanics
9.11 Actin-Binding Proteins
9.12 Cellular Motility
9.13 The Bacterial Cytoskeleton
Analytic Questions
CHAPTER 10: The Nature of the Gene and the Genome
10.1 The Concept of a Gene as a Unit of Inheritance
10.2 The Discovery of Chromosomes
10.3 Chromosomes as the Carriers of Genetic Information
10.4 The Chemical Nature of the Gene
10.5 The Complexity of the Genome
10.6 The Stability of the Genome
10.7 Sequencing Genomes: The Footprints of Biological Evolution
 10.8 Engineering Linkage: Engineering Genomes
10.9 The Genetic Basis of “Being Human”
10.10 Green Cells: Gene Transfer by Agrobacterium tumefaciens
Analytic Questions
CHAPTER 11: The Central Dogma: DNA to RNA to Protein
11.1 The Relationships among Genes, Proteins, and RNAs
11.2 An Overview of Transcription in Both Prokaryotic and Eukaryotic Cells
11.3 Synthesis and Processing of Eukaryotic Ribosomal and Transfer RNAs
11.4 Synthesis and Structure of Eukaryotic Messenger RNAs
11.5 Small Regulatory RNAs and RNA Silencing Pathways
11.6 Green Cells: Long-Range siRNA Movement
11.7 CRISPR and Other Noncoding RNAs
11.8 Encoding Genetic Information
11.9 Decoding the Codons: The Role of Transfer RNAs
11.10 Translating Genetic Information
11.11 Engineering Linkage: DNA Origami
Analytic Questions
CHAPTER 12: Control of Gene Expression
12.1 Control of Gene Expression in Bacteria
12.2 Engineering Linkage: Building Digital Logic with Genes
12.3 Structure of the Nuclear Envelope
12.4 Chromosomes and Chromatin
12.5 The Nucleus as an Organized Organelle
12.6 An Overview of Gene Regulation in Eukaryotes
12.7 Transcriptional Control
12.8 Green Cells: The ABC Model and MADS Domain Transcription Factors
12.9 RNA Processing Control
12.10 Translational Control
12.11 Posttranslational Control: Determining Protein Stability
Analytic Questions
CHAPTER 13: DNA Replication and Repair
13.1 DNA Replication
13.2 DNA Replication in Bacterial Cells
13.3 The Structure and Functions of DNA Polymerases
13.4 Replication in Viruses
13.5 Engineering Linkage: Storing Data in DNA
13.6 DNA Replication in Eukaryotic Cells
13.7 DNA Repair
 13.8 Green Cells: Gamma Gardens
13.9 Between Replication and Repair
Analytic Questions
CHAPTER 14: Cell Division
14.1 The Cell Cycle
14.2 M Phase: Mitosis and Cytokinesis
14.3 Engineering Linkage: The Role of Membrane Tension in Cell Division
14.4 Green Cells: Unique Aspects of Plant Cell Division
14.5 Meiosis
Analytic Questions
CHAPTER 15: Cell Signaling and Signal Transduction: Communication between Cells
15.1 The Basic Elements of Cell Signaling Systems
15.2 A Survey of Extracellular Messages and Their Receptors
15.3 G Protein-Coupled Receptors and Their Second Messengers
15.4 Engineering Linkage: Biosensors in Medicine and Biology
15.5 Protein-Tyrosine Phosphorylation as a Mechanism for Signal Transduction
15.6 Green Cells: Auxin Signaling
15.7 The Role of Calcium as an Intracellular Messenger
15.8 Convergence, Divergence, and Cross-Talk among Different Signaling Pathways
15.9 The Role of NO as an Intracellular Messenger
15.10 Apoptosis (Programmed Cell Death)
Analytic Questions
CHAPTER 16: Cancer
16.1 Basic Properties of a Cancer Cell
16.2 The Causes of Cancer
16.3 Cancer: A Genetic Disorder
16.4 Engineering Linkage: Therapeutic Radiation
16.5 Green Cells: Plant-Based Chemotherapies
16.6 Strategies for Combating Cancer
CHAPTER 17: The Immune Response
17.1 An Overview of the Immune Response
17.2 Green Cells: The Plant Immune System
17.3 The Clonal Selection Theory as It Applies to B Cells
17.4 T Lymphocytes: Activation and Mechanism of Action
17.5 Selected Topics on the Cellular and Molecular Basis of Immunity
17.6 Engineering Linkage: Adoptive T-Cell Therapy
17.7 Signal Transduction Pathways in Lymphocyte Activation
CHAPTER 18: Techniques in Cell and Molecular Biology
 18.1 The Light Microscope
18.2 Transmission Electron Microscopy
18.3 Scanning Electron and Atomic Force Microscopy
18.4 The Use of Radioisotopes
18.5 Cell Culture
18.6 The Fractionation of a Cell’s Contents by Differential Centrifugation
18.7 Isolation, Purification, and Fractionation of Proteins
18.8 Determining the Structure of Proteins and Multisubunit Complexes
18.9 Fractionation of Nucleic Acids
18.10 Nucleic Acid Hybridization
18.11 Chemical Synthesis of DNA
18.12 Recombinant DNA Technology
18.13 Enzymatic Amplification of DNA by PCR
18.14 DNA Sequencing
18.15 DNA Libraries
18.16 DNA Transfer into Eukaryotic Cells and Mammalian Embryos
18.17 Gene Editing and Silencing
18.18 The Use of Antibodies
Additional Readings
Glossary
Index
End User License Agreement

List of Tables
CHAPTER 1
TABLE 1.1 A Comparison of Prokaryotic and Eukaryotic Cells
TABLE 1.2 Number and Biomass of Prokaryotes in the World
CHAPTER 2
TABLE 2.1 Strengths of Acids and Bases
TABLE 2.2 Functional Groups
CHAPTER 3
TABLE 3.1 Thermodynamics of the Water–Ice Transformation
TABLE 3.2 Relation between ΔG°' and K'eq at 25°C
TABLE 3.3 Catalytic Activity of a Variety of Enzymes
TABLE 1 Antibiotics in Clinical Use and Modes of Resistance
CHAPTER 4
 TABLE 4.1 Lipid Compositions of Some Biological Membranes
TABLE 4.2 Melting Points of the Common 18-Carbon Fatty Acids
TABLE 4.3 Ion Concentrations Inside and Outside a Typical Mammalian Cell
CHAPTER 5
TABLE 5.1 Standard Redox Potentials of Selected Half-Reactions
CHAPTER 7
TABLE 7.1 Classification of Integrin Receptors Based on Recognition of RGD
Seque...
CHAPTER 8
TABLE 1 Sphingolipid Storage Diseases
TABLE 8.1 A Sampling of Lysosomal Enzymes
CHAPTER 9
TABLE 9.1 Properties of Microtubules, Intermediate Filaments, and Actin
Filaments
TABLE 9.2 Properties and Distribution of the Major Mammalian Intermediate
Filame...
CHAPTER 10
TABLE 10.1 Seven Traits of Mendel’s Pea Plants
CHAPTER 11
TABLE 11.1 Eukaryotic Nuclear RNA Polymerases
CHAPTER 13
TABLE 13.1 Some of the Proteins Required for Replication
CHAPTER 15
TABLE 15.1 Examples of Physiologic Processes Mediated by GPCRs and
Heterotrimeric G Proteins
TABLE 1 Effects of Combinations of Hormones, at Supramaximal Concentrations,
on Adenylyl...
TABLE 2 Purification of the Regulatory Component of Adenylyl Cyclase from
Rabbit Liver
TABLE 1 Human Diseases Linked to the G Protein Pathway
TABLE 15.2 Summary of Cellular Responses Elicited by Adding IP3 to Either
Permeabilized or...
TABLE 15.3 Examples of Hormone-Induced Responses Mediated by cAMP
TABLE 15.4 Examples of Mammalian Proteins Activatedby Ca2+
CHAPTER 16
TABLE 1 Characterization of the Polymerase Product
 TABLE 16.1 Tumor-Suppressor Genes
TABLE 16.2 Examples of Small-Molecule Targeted Therapies That Either Have
Been FDA-Approved...
CHAPTER 17
TABLE 17.1 Selected Cytokines
TABLE 17.2 Classes of Human Immunoglobulins
TABLE 1 Cytotoxic Activity of Spleen Cells from Various Strains of Mice Injected 7
Days ...
TABLE 2 Inhibition of Antigen Presentation with NH4Cl and Chloroquine
CHAPTER 18
TABLE 18.1 Properties of a Variety of Radioisotopes Used in Biological Research

List of Illustrations
CHAPTER 1
FIGURE 1.1 The discovery of cells. (a) One of Robert Hooke’s more ornate
compound (double-l...
FIGURE 1.2 HeLa cells, such as the ones pictured here, were the first human cells
to be kep...
FIGURE 1.3 Levels of cellular and molecular organization. The brightly colored
photograph o...
FIGURE 1.4 Cell reproduction. This mammalian oocyte has recently undergone a
highly unequal...
FIGURE 1.5 Acquiring energy. A living cell of the filamentous alga Spirogyra. The
ribbon-li...
FIGURE 1.6 Self-regulation. The left panel depicts the normal development of a
sea urchin i...
FIGURE 1.7 Cellular activities are often analogous to this Rube Goldberg machine
in which o...
FIGURE 1.8 The structure of cells. Schematic diagrams of a “generalized” bacterial
(a), pla...
FIGURE 1.9 Earth’s biogeologic clock. A portrait of the past five billion years of
Earth’s ...
FIGURE 1.10 The structure of a eukaryotic cell. This epithelial cell lines the male
reproduc...
FIGURE 1.11 The cytoplasm of a eukaryotic cell is a crowded compartment. This
colorized elec...
FIGURE 1.12 Cell division in eukaryotes requires the assembly of an elaborate
chromosome-sep...
 FIGURE 1.13 Bacterial conjugation. Electron micrograph showing a conjugating
pair of bacteri...
FIGURE 1.14 The difference between prokaryotic and eukaryotic flagella. (a) The
bacterium Sa...
FIGURE 1.15 Cyanobacteria. (a) Electron micrograph of a cyanobacterium
showing the cytoplasm...
FIGURE 1.16 Vorticella, a complex ciliated protist. A number of these unicellular
organisms ...
FIGURE 1.17 Pathways of cell differentiation. A few of the types of differentiated
cells pre...
FIGURE 1 An adult muscle stem cell. (a) A portion of a muscle fiber, with its many
nuclei...
FIGURE 2 Embryonic stem cells; their isolation and potential use. (a) Micrograph
of a mam...
FIGURE 3 Steps taken to generate induced pluripotent stem (iPS) cells for use in
correcti...
FIGURE 1.18 Six model organisms. (a) Escherichia coli is a rod-shaped bacterium
that lives i...
FIGURE 1.19 Relative sizes of cells and cell components. These structures differ in
size by ...
FIGURE 1.20 The synthetic biologist’s toolkit of the future? Such a toolkit would
presumably.
FIGURE 1.21 Tobacco mosaic virus (TMV). (a) Model of a portion of a TMV
particle. The protei...
FIGURE 1.22 Virus diversity. The structures of (a) an adenovirus, (b) a human
immunodeficien...
FIGURE 1.23 A virus infection. (a) Micrograph showing a late stage in the
infection of a bac...
FIGURE 1 A model depicting stages in the evolution of eukaryotes. Starting from a
prokary...
FIGURE 2 Prokaryotes with complex internal membrane systems. Electron
micrograph of Gemma...
FIGURE 3 Domains of life. (a) A phylogenetic tree based on rRNA sequence
comparisons show...
FIGURE 1.24 Evolutionary experiments in multicelluarity. (a) Volvox carteri, a
multicellular...
FIGURE 1.25 Replacement blood vessel that incorporates living cells, created
using tissue en...
CHAPTER 2
FIGURE 2.1 A representation of the arrangement of electrons in a number of
common atoms. El...
FIGURE 2.2 Gamma knife machine. Left panel shows hemispherical array of
cobalt ingots, each...
FIGURE 2.3 The dissolution of a salt crystal. When placed in water, the Na+ and
Cl− ions of...
FIGURE 2.4 Noncovalent ionic bonds play an important role in holding the
protein molecule o...
FIGURE 2.5 Hydrogen bonds form between a bonded electronegative atom, such
as nitrogen or o...
FIGURE 2.6 In a hydrophobic interaction, the nonpolar (hydrophobic) molecules
are forced in...
FIGURE 2.7 Van der Waals forces. (a) As two atoms approach each other, they
experience a we...
FIGURE 2.8 Hydrogen bond formation between neighboring water molecules.
Each H atom of the ...
FIGURE 2.9 The importance of water in protein structure. The water molecules
(each with a s...
FIGURE 2.10 The structure of cholesterol illustrates how carbon atoms
(represented by the bl...
FIGURE 2.11 Monomers and polymers; polymerization and hydrolysis. (a)
Polysaccharides, prote...
FIGURE 2.12 An overview of the types of biological molecules that make up
various cellular s...
FIGURE 2.13 Fertilizers, both organic and chemical, provide elements such as
nitrogen and ph...
FIGURE 2.14 The structures of sugars. (a) Straight-chain formula of fructose, a
ketohexose [...
FIGURE 2.15 Stereoisomerism of glyceraldehyde. (a) The four groups bonded to a
carbon atom (...
FIGURE 2.16 Aldotetroses. Because they have two asymmetric carbon atoms,
aldotetroses can ex...
FIGURE 2.17 Formation of an α- and β-pyranose. When a molecule of glucose
undergoes self-rea...
FIGURE 2.18 Disaccharides. Sucrose and lactose are two of the most common
disaccharides. Suc...
FIGURE 2.19 Three polysaccharides with identical sugar monomers but
dramatically different p...
FIGURE 2.20 Chitin is the primary component of the outer skeleton of this
grasshopper....
FIGURE 2.21 Fats and fatty acids. (a) The basic structure of a triacylglycerol (also
called ...
FIGURE 2.22 Soaps consist of fatty acids. In this schematic drawing of a soap
micelle, the n...
FIGURE 2.23 The structure of steroids. All steroids share the basic four-ring
skeleton. The ...
FIGURE 2.24 The phospholipid phosphatidylcholine. The molecule consists of a
glycerol backbo...
FIGURE 2.25 Four examples of the thousands of biological structures composed
predominantly o...
FIGURE 2.26 Amino acid structure. Ball-and-stick model (a) and chemical
formula (b) of a gen...
FIGURE 2.27 Amino acid stereoisomerism. Because the α-carbon of all amino
acids except glyci...
FIGURE 2.28 The chemical structure of amino acids. These 20 amino acids
represent those most...
FIGURE 2.29 The ionization of charged, polar amino acids. (a) The side chain of
glutamic aci...
FIGURE 2.30 Disposition of hydrophilic and hydrophobic amino acid residues in
the soluble pr...
FIGURE 2.31 Scanning electron micrograph of a red blood cell from a person with
sickle cell ...
FIGURE 2.32 The alpha helix. (a) The helical path around a central axis taken by
the polypep...
FIGURE 2.33 The β sheet. (a) Each polypeptide of a β sheet assumes an extended
but pleated c...
FIGURE 2.34 A ribbon model of ribonuclease. The regions of α helix are depicted
as spirals a...
FIGURE 2.35 An X-ray diffraction pattern of myoglobin. The pattern of spots is
produced as a...
FIGURE 2.36 NMR spectroscopy reveals tertiary structure without crystalization.
(a) An NMR s...
FIGURE 2.37 The three-dimensional structure of myoglobin. Most of the amino
acids in the ter...
FIGURE 2.38 Types of noncovalent bonds maintaining the conformation of
proteins....
FIGURE 2.39 Different sequence, similar structure. Two proteins, actin and MreB,
with primar...
FIGURE 2.40 Proteins are built of structural units, or domains. The mammalian
enzyme phospho...
FIGURE 2.41 Dynamic movements within the enzyme acetylcholinesterase. A
portion of the enzym...
FIGURE 2.42 Proteins with quaternary structure. (a) Ribbon diagram of
transforming growth fa...
FIGURE 2.43 Pyruvate dehydrogenase: a multiprotein complex. (a) Three-
dimensional reconstruc...
FIGURE 2.44 Protein–protein interactions. (a) A model illustrating the
complementary molecul...
FIGURE 2.45 Denaturation and refolding of ribonuclease. A native ribonuclease
molecule (with...
FIGURE 2.46 Two alternate pathways by which a newly synthesized or denatured
protein could a...
FIGURE 2.47 Along the folding pathway. The image on the left shows the native
tertiary struc...
FIGURE 1 A contrast in structure. (a) Tertiary structure of the normal (PrPC)
protein as...
FIGURE 2 Alzheimer’s disease. (a) The defining characteristics of brain tissue from
a per...
FIGURE 3 Formation of the Aβ peptide. The Aβ peptide is carved from the amyloid
precursor...
FIGURE 4 A neuroimaging technique that reveals the presence of amyloid in the
brain. Thes...
FIGURE 2.48 The role of molecular chaperones in encouraging protein folding.
The steps are d...
FIGURE 1 An early model of the GroEL complex built according to data from
electron micros...
FIGURE 2 Reconstructions of GroEL based on high-resolution electron
micrographs of specim...
FIGURE 3 Conformational change in GroEL. (a) The model on the left shows a
surface view o...
FIGURE 4 A schematic illustration of the proposed steps that occur during the
GroEL-GroES...
FIGURE 2.49 Identifying proteins by mass spectrometry. A protein is isolated
from a cell or ...
FIGURE 2.50 A network of protein–protein interactions. Each red line represents
an interacti...
FIGURE 2.51 Protein–protein interactions of hub proteins. (a) The enzyme RNA
polymerase II, ...
FIGURE 2.52 The computational design of a protein that is capable of binding
specifically to...
 FIGURE 2.53 Development of a protein-targeting drug, such as Gleevec. (a)
Typical steps in d...
FIGURE 2.54 Distribution of polar, charged amino acid residues in the enzyme
malate dehydrog...
FIGURE 2.55 The dramatic effect on conformation that can result from a single
amino acid sub...
FIGURE 2.56 Nucleotides and nucleotide strands of RNA. (a) Nucleotides are the
monomers from...
FIGURE 2.57 Nitrogenous bases in nucleic acids. Of the four standard bases found
in RNA, ade...
FIGURE 2.58 RNAs can assume complex shapes. (a) This ribosomal RNA is an
integral component ...
FIGURE 2.59 Reconstruction of a ribosome from the cytoplasm of a wheat germ
cell. This recon...
FIGURE 2.60 Example of a phase-separated compartment formed by Whi3, an
RNA-binding protein ...
CHAPTER 3
FIGURE 3.1 Examples of energy transduction. (a) Conversion of mechanical
energy to electric...
FIGURE 3.2 A change in a system’s internal energy. In this example, the system is
defined a...
FIGURE 3.3 Events are accompanied by an increase in the entropy of the universe.
(a) A suga...
FIGURE 3.4 When water freezes, its entropy decreases because the water
molecules of ice exi...
FIGURE 3.5 ATP hydrolysis. Adenosine triphosphate (ATP) is hydrolyzed as part
of many bioch...
FIGURE 3.6 A few roles for ATP hydrolysis. In the cell, energy from ATP
hydrolysis may be u...
FIGURE 3.7 Steady state versus equilibrium. (a) As long as this ameba can
continue to take ...
FIGURE 3.8 Activation energy and enzymatic reactions. Even though the
formation of glucose ...
FIGURE 3.9 The effect of lowering activation energy on the rate of a reaction. The
bell-sha...
FIGURE 3.10 Formation of an enzyme–substrate complex. Schematic drawing of
the reaction cata...
FIGURE 3.11 The active site of an enzyme. (a) Diagrammatic representation of the
active site...
FIGURE 3.12 Three mechanisms by which enzymes accelerate reactions: (a)
maintaining precise ...
FIGURE 3.13 Diagrammatic representation of the catalytic mechanism of
chymotrypsin. The reac...
FIGURE 3.14 An example of induced fit. When a glucose molecule binds to the
enzyme hexokinas...
FIGURE 3.15 Electron density map of a single hydrogen bond (green-dotted line).
This map sho...
FIGURE 3.16 Myoglobin: the movie. In this example of time-resolved X-ray
crystallography, th...
FIGURE 3.17 The relationship between the rate (velocity) of an enzyme-catalyzed
reaction and...
FIGURE 3.18 A Lineweaver-Burk plot of the reciprocals of velocity and substrate
concentratio...
FIGURE 3.19 Dependence of the rate of an enzyme-catalyzed reaction on (a) pH,
and (b) temper...
FIGURE 3.20 Competitive inhibition. Because of their molecular similarity,
competitive inhib...
FIGURE 3.21 The effects of inhibitors on enzyme kinetics. The effect of both
competitive and...
FIGURE 3.22 Three stages of metabolism. The catabolic pathways (green arrows
rightward) conv...
FIGURE 3.23 The oxidation state of a carbon atom depends on the other atoms to
which it is b...
FIGURE 3.24 The steps of glycolysis....
FIGURE 3.25 Free-energy profile of glycolysis in cardiac muscle tissue. The step
numbers cor...
FIGURE 3.26 The transfer of energy during chemical oxidation. The oxidation of
glyceraldehyd...
FIGURE 3.27 The structure of NAD+ and its reduction to NADH. When the 2′ OH
of the ribose mo...
FIGURE 3.28 Ranking compounds by phosphate transfer potential. Those
phosphorylated compound...
FIGURE 3.29 Fermentation. Most cells carry out aerobic respiration, which
depends on molecul...
FIGURE 3.30 Feedback inhibition. Starting with two substrates, A and B, a series
of three en...
FIGURE 3.31 Glycolysis versus gluconeogenesis. Whereas most of the reactions
are the same in...
FIGURE 3.32 In the silk plant (Albizia julibrissin), leaves extend to collect light
 during t...
FIGURE 3.33 Brain tumor visualized using PET scanning to detect accumulation
of 18F-FDG. Red...
CHAPTER 4
FIGURE 4.1 The trilaminar appearance of membranes. (a) Electron micrograph
showing the thre...
FIGURE 4.2 A summary of membrane functions in a plant cell. (1) An example of
membrane comp...
FIGURE 4.3 The plasma membrane contains a lipid bilayer. (a) Calculating the
surface area o...
FIGURE 4.4 Plasma membranes as lipids plus proteins. (a) A representation of the
plasma mem...
FIGURE 4.5 The myelin sheath. Electron micrograph of a nerve cell axon
surrounded by a myel...
FIGURE 4.6 The chemical structures of membrane lipids. (a) The structures of
phosphoglyceri...
FIGURE 4.7 The cholesterol molecules (shown in green) of a lipid bilayer are
oriented with ...
FIGURE 4.8 The dynamic properties of the plasma membrane. (a) The leading
edge of a moving ...
FIGURE 4.9 Liposomes. A schematic diagram of a stealth liposome containing a
hydrophilic po...
FIGURE 4.10 The asymmetric distribution of phospholipids (and cholesterol) in
the plasma mem...
FIGURE 4.11 Two types of linkages that join sugars to a polypeptide chain. The
N-glycosidic ...
FIGURE 4.12 Blood group antigens. Whether a person has type A, B, AB, or O
blood is determin...
FIGURE 4.13 Three classes of membrane proteins. (a) Integral proteins typically
contain one ...
FIGURE 4.14 The interactions between membrane proteins and lipids. (a)
Aquaporin is a membra...
FIGURE 4.15 Freeze fracture: a technique for investigating cell membrane
structure. (a) When...
FIGURE 4.16 Solubilization of membrane proteins with detergents. The nonpolar
ends of the de...
FIGURE 4.17 Structure of integral proteins. (a) Tertiary structure of the
photosynthetic rea...
FIGURE 4.18 Glycophorin A, an integral protein with a single transmembrane
domain. The singl...
FIGURE 4.19 Accommodating various amino acid residues within transmembrane
helices. (a) In t...
FIGURE 4.20 Hydropathy plot for glycophorin A, a single membrane-spanning
protein. Hydrophob...
FIGURE 4.21 An experiment employing site-directed mutagenesis to learn about
dynamic changes...
FIGURE 4.22 Use of EPR spectroscopy to monitor changes in conformation of a
bacterial K+ ion ...
FIGURE 4.23 The structure of the lipid bilayer depends on the temperature. The
bilayer shown...
FIGURE 4.24 Lipid rafts. (a) Image of the upper surface of an artificial lipid
bilayer conta...
FIGURE 4.25 The possible movements of phospholipids in a membrane. The
figure shows the type...
FIGURE 4.26 The use of cell fusion to reveal the mobility of membrane proteins.
(a) Outline ...
FIGURE 4.27 Measuring the diffusion rates of membrane proteins by fluorescence
recovery afte...
FIGURE 4.28 Patterns of movement of integral membrane proteins. Depending
on the cell type a...
FIGURE 4.29 Experimental demonstration that diffusion of phospholipids within
the plasma mem...
FIGURE 4.30 Differentiated functions of the plasma membrane of an epithelial
cell. The apica...
FIGURE 4.31 Differentiation of the mammalian sperm plasma membrane as
revealed by fluorescen...
FIGURE 4.32 The plasma membrane of the human erythrocyte. (a) Scanning
electron micrograph o...
FIGURE 4.33 Four basic mechanisms by which solute molecules move across
membranes. The relat...
FIGURE 4.34 The relationship between partition coefficient and membrane
permeability. In thi...
FIGURE 4.35 The effects of differences in the concentration of solutes on opposite
sides of ...
FIGURE 4.36 The effects of osmosis on a plant cell. (a) Aquatic plants living in
fresh water...
FIGURE 4.37 Passage of water molecules through an aquaporin channel. (a)
Snapshot from a mol...
FIGURE 4.38 Measuring ion channel conductance by patch-clamp recording. (a)
In this techniqu...
FIGURE 4.39 Three-dimensional structure of the bacterial KcsA channel and the
selection of K+ ...
FIGURE 4.40 Schematic illustration of the hinge-bending model for the opening
of the KcsA ch...
FIGURE 4.41 The structure of one subunit of a eukaryotic, voltage-gated K+
channel. A two-di...
FIGURE 4.42 Three-dimensional structure of a voltage-gated mammalian K+
channel. (a) The cry...
FIGURE 4.43 Conformational states of a voltage-gated K+ ion channel. (a) Three-
dimensional m...
FIGURE 1 The electric organs of Torpedo consist of stacks of modified
neuromuscular junct...
FIGURE 2 Steps used in the isolation of the nAChR. (a) Structure of a synthetic
compound,...
FIGURE 3 The top portion of the figure shows an SDS–polyacrylamide gel
following electrop...
FIGURE 4 Electron micrograph of negatively stained, receptor-rich membranes
from the elec...
FIGURE 5 (a) An electron density map of a slice through nAChR obtained by
analyzing elect...
FIGURE 6 Ribbon drawings illustrating the changes that occur within the nAChR
conducting ...
FIGURE 4.44 Facilitated diffusion. A schematic model for the facilitated diffusion
of glucos...
FIGURE 4.45 The kinetics of facilitated diffusion compared to that of simple
physical diffus...
FIGURE 4.46 The Na+/K+-ATPase. (a) Simplified schematic model of the
transport cycle as desc...
FIGURE 4.47 Control of acid secretion in the stomach. In the resting state, the H+
/ K+-ATPase...
FIGURE 1 An explanation for the debilitating effects on lung function from the
absence of...
FIGURE 4.48 Bacteriorhodopsin: a light-driven proton pump. The protein
contains seven membra...
FIGURE 4.49 Secondary transport: the use of energy stored in an ionic gradient.
+
The Na+ /K ...
FIGURE 4.50 A schematic model of the transport cycle of a secondary transporter.
Four differ...
FIGURE 4.51 The structure of a nerve cell. (a) Schematic drawing of a simple
 neuron with a m...
FIGURE 4.52 Measuring a membrane’s resting potential. A potential is measured
when a differe...
FIGURE 4.53 Formation of an action potential. (a) Time 1, upper left box: The
membrane in th...
FIGURE 4.54 Propagation of an impulse results from the local flow of ions. An
action potenti...
FIGURE 4.55 Saltatory conduction. During saltatory conduction, only the
membrane in the noda...
FIGURE 4.56 The neuromuscular junction is the site where branches from a
motor axon form syn...
FIGURE 4.57 The sequence of events during synaptic transmission with
acetylcholine as the ne...
FIGURE 4.58 Action potentials in plant cells. (a) The Venus flytrap catches insects
in a tra...
FIGURE 4.59 Cochlear implant showing a flexible silicone elastomer containing
platinum elect...
CHAPTER 5
FIGURE 5.1 Mitochondria. (a) A living fibroblast viewed with a phase-contrast
microscope. M...
FIGURE 5.2 Mitochondrial fusion and fission. (a) The dynamic nature of these
organelles is ...
FIGURE 5.3 The structure of a mitochondrion. (a) Scanning electron micrograph
of a macerate...
FIGURE 5.4 Porins. Gram-negative bacteria have a lipid-containing outer
membrane outside of...
FIGURE 5.5 An overview of carbohydrate metabolism in eukaryotic cells. The
reactions of gly...
FIGURE 5.6 An overview of glycolysis showing some of the key steps. These
include the two r...
FIGURE 5.7 The tricarboxylic acid (TCA) cycle. The cycle begins with the
condensation of ox...
FIGURE 5.8 Catabolic pathways generate compounds that are fed into the TCA
cycle. (a) Oxida...
FIGURE 5.9 The glycerol phosphate shuttle. In the glycerol phosphate shuttle,
electrons are...
FIGURE 5.10 A summary of the process of oxidative phosphorylation. In the first
step of the ...
FIGURE 1 Skeletal muscles contain a mix of fast-twitch (or type II) fibers (darkly
staine...
FIGURE 5.11 Measuring the standard oxidation–reduction (redox) potential. The
sample half-ce...
FIGURE 5.12 Structures of the oxidized and reduced forms of three types of
electron carriers...
FIGURE 5.13 Iron-sulfur centers. Structures of (a) [2F e-2S] and (b) [4Fe-4S] iron-
sulfur cen...
FIGURE 5.14 The arrangement of several carriers in the electron-transport chain.
The diagram...
FIGURE 5.15 Experimental use of inhibitors to determine the sequence of carriers
in the elec...
FIGURE 5.16 Electron-tunneling pathways for the yeast cytochrome c-cytochrome
c peroxidase c...
FIGURE 5.17 The electron-transport chain of the inner mitochondrial membrane.
The respirator...
FIGURE 5.18 Experimental demonstration that cytochrome oxidase is a proton
pump. When purifi...
FIGURE 5.19 Structure and a proposed mechanism of action of complex I of the
respiratory cha...
FIGURE 5.20 A summary of cytochrome oxidase activity. A model showing the
flow of electrons ...
FIGURE 5.21 Pulse oximeter. Red and infrared light emitting diodes transmit light
through th...
FIGURE 5.22 Visualizing the proton-motive force. Fluorescence micrograph of a
cultured cell ...
FIGURE 5.23 The machinery for ATP synthesis. Three-dimensional electron
micrograph of isolat...
FIGURE 5.24 An experiment to drive ATP formation in membrane vesicles
reconstituted with the...
FIGURE 5.25 The structure of ATP synthase. (a) Schematic diagram of the ATP
synthase from...
FIGURE 5.26 Visualizing the oligomeric c ring of a chloroplast ATP synthase.
Atomic force mi...
FIGURE 5.27 The structural basis of catalytic site conformation. (a) A section
through the F...
FIGURE 5.28 The binding change mechanism for ATP synthesis. (a) Schematic
drawing showing ch...
FIGURE 5.29 Direct observation of rotational catalysis. (a) To carry out the
experiment, a m...
FIGURE 5.30 A model in which proton diffusion is coupled to the rotation of the c
ring of the...
 FIGURE 5.31 Summary of the major activities during aerobic respiration in a
mitochondrion.
FIGURE 5.32 The structure and function of peroxisomes. (a) Electron micrograph
of a section ...
FIGURE 1 Mitochondrial abnormalities in skeletal muscle. (a) Ragged-red fibers.
These deg...
FIGURE 2 A premature aging phenotype caused by increased mutations in
mtDNA. The photogra...
FIGURE 5.33 Glyoxysome localization within plant seedlings. Light micrograph of
a section th...
CHAPTER 6
FIGURE 6.1 Photosynthetic green sulfur bacteria are present as a ring of
peripheral cells t...
FIGURE 6.2 The functional organization of a leaf. The section of the leaf shows
several lay...
FIGURE 6.3 The internal structure of a chloroplast. (a) Transmission electron
micrograph th...
FIGURE 6.4 Thylakoid membranes. Electron micrograph of a section through a
portion of a chl...
FIGURE 6.5 An overview of the energetics of photosynthesis and aerobic
respiration....
FIGURE 6.6 The structure of chlorophyll a. The molecule consists of a porphyrin
ring (which...
FIGURE 6.7 Absorption spectrum for several photosynthetic pigments of higher
plants. The ba...
FIGURE 6.8 Action spectrum for photosynthesis. The action spectrum (red line)
indicates the...
FIGURE 6.9 Chromoplasts within the cells of a red pepper....
FIGURE 6.10 The transfer of excitation energy. Energy is transferred randomly
through a netw...
FIGURE 6.11 An overview of the flow of electrons during the light-dependent
reactions of pho...
FIGURE 6.12 The functional organization of photosystem II. (a) A schematic
model of the huge...
FIGURE 6.13 Plastoquinone. The acceptance of two electrons and two protons
reduces PQ (plast...
FIGURE 6.14 Measuring the kinetics of O2 release. The plot shows the response by
isolated ch...
FIGURE 6.15 Electron transport between PSII and PSI. The flow of a pair of
electrons is indi...
 FIGURE 6.16 The functional organization of photosystem I. The path taken by
electrons is ind...
FIGURE 6.17 Summary of the light-dependent reactions. (a) Three-dimensional
structures of th...
FIGURE 6.18 Simplified scheme for cyclic photophosphorylation. Absorption of
light by PSI ex...
FIGURE 6.19 Chromatogram showing the results of an experiment in which algal
cells were incu...
FIGURE 6.20 Converting CO2 into carbohydrate. (a) The reaction catalyzed by
ribulose bisphos...
FIGURE 6.21 An overview of the various stages of photosynthesis....
FIGURE 6.22 Redox control of the Calvin cycle. In the light, ferredoxin is reduced,
and a fr...
FIGURE 6.23 The reactions of photorespiration. Rubisco can catalyze two
different reactions ...
FIGURE 6.24 The cellular basis of photorespiration. Electron micrograph of a
portion of a le...
FIGURE 6.25 Structure and function in C4 plants. Electron micrograph of a
transverse section...
FIGURE 6.26 Aminolevulinic acid (ALA) is converted to the photosensitizing
agent protoporphy...
CHAPTER 7
FIGURE 7.1 An overview of cell organization into tissues and of their interactions
with one...
FIGURE 7.2 The glycocalyx. (a) The basal surface of an ectodermal cell of an early
chick em...
FIGURE 7.3 The extracellular matrix (ECM) of cartilage cells. (a) Scanning
electron microgr...
FIGURE 7.4 The basement membrane (basal lamina). (a) Scanning electron
micrograph of human ...
FIGURE 7.5 An overview of the macromolecular organization of the extracellular
matrix. The ...
FIGURE 7.6 The structure of collagen I. This figure depicts several levels of
organization ...
FIGURE 7.7 The corneal stroma consists largely of layers of collagen fibrils of
uniform dia...
FIGURE 7.8 The type IV collagen network of the basement membrane. Electron
micrograph of a ...
FIGURE 7.9 The structure of a cartilage-type proteoglycan complex. (a) Schematic
representa...
FIGURE 7.10 Structure of fibronectin and its importance during embryonic
development. (a) A ...
FIGURE 7.11 The role of cell migration during embryonic development. (a) A
summary of some o...
FIGURE 7.12 A model of the basement membrane scaffold. Basement membranes
contain two networ...
FIGURE 7.13 Fluorescence microscopy image of a brain organoid. Neurons,
labeled green, are e...
FIGURE 7.14 Integrin conformations. (a) Schematic drawing of a complete
integrin in the bent...
FIGURE 7.15 The role of integrins in platelet aggregation. (a) Blood clots form
when platele...
FIGURE 7.16 Steps in the process of cell spreading. Scanning electron
micrographs showing th...
FIGURE 7.17 Focal adhesions are sites where cells adhere to their substratum and
transmit si...
FIGURE 7.18 Experimental demonstration of forces exerted by focal adhesions.
Scanning-electr...
FIGURE 7.19 Measuring the force necessary to activate integrins. In this
experiment, an inte...
FIGURE 7.20 Hemidesmosomes. Hemidesmosomes are differentiated sites at the
basal surfaces of...
FIGURE 7.21 Experimental demonstration of cell–cell recognition. When cells
from different p...
FIGURE 7.22 Overview of cell adhesion molecules. (a) Selectins. All three types of
known sel...
FIGURE 1 Steps in the movement of neutrophils from the bloodstream during
inflammation. T...
FIGURE 2 Steps leading to the metastatic spread of an epithelial cancer (a
carcinoma). (a...
FIGURE 7.23 Cadherins and morphogenesis. (a) During gastrulation, cells in the
upper layer o...
FIGURE 7.24 Cadherins form tip links of stereocilia. Cadherin 23 and
protocadherin 15 form t...
FIGURE 7.25 An intercellular junctional complex. (a) Schematic diagram showing
the junctiona...
FIGURE 7.26 Schematic model of the molecular architecture of an adherens
junction and desomo...
FIGURE 7.27 Specialized cadherins, called desmoglein and desmocollin, bind to
one another in...
 FIGURE 7.28 Tight junctions. (a) Electron micrograph of a section through the
apical region ...
FIGURE 7.29 The molecular composition of tight junction strands. Electron
micrograph of a fr...
FIGURE 7.30 Gap junctions. (a) Electron micrograph of a section through a gap
junction perpe...
FIGURE 7.31 Results of an experiment demonstrating the passage of low-
molecular-weight solut...
FIGURE 1 Micrograph showing recording microelectrodes being inserted into
living cells of...
FIGURE 2 Calcium waves induced by mechanical stimulation in (a) a control
culture of rat ...
FIGURE 3 (a) When a small mass of C6 glioma cells is implanted into the brain of a
rat, t...
FIGURE 7.32 Plasmodesmata. (a) Electron micrograph of a section through a
plasmodesma of a f...
FIGURE 7.33 Tunneling nanotubes. Scanning electron micrograph showing two
cultured neuroendo...
FIGURE 7.34 The plant cell wall. (a) Electron micrograph of a plant cell
surrounded by its c...
FIGURE 7.35 Synthesis of plant cell wall macromolecules. (a) Freeze-fracture
replica of the ...
CHAPTER 8
FIGURE 8.1 Membrane-bound compartments of the cytoplasm. The cytoplasm of
this root cap cel...
FIGURE 8.2 An overview of the biosynthetic/secretory and endocytic pathways
that unite endo...
FIGURE 8.3 Autoradiography reveals the sites of synthesis and subsequent
transport of secre...
FIGURE 8.4 The use of green fluorescent protein (GFP) reveals the movement of
proteins with...
FIGURE 8.5 Microscopic images of a mammalian cell expressing multiple
fluorophores to visua...
FIGURE 8.6 Isolation of a microsomal fraction by differential centrifugation. (a)
When a ce...
FIGURE 8.7 Formation of coated vesicles in a cell-free system. Electron
micrograph of a lip...
FIGURE 8.8 The use of genetic mutants in the study of secretion. (a) The first leg
of the b...
FIGURE 8.9 Inhibition of gene expression with RNA interference. (a) A control
Drosophila S2...
FIGURE 8.10 The rough endoplasmic reticulum (RER). (a) Schematic diagram
showing the stacks ...
FIGURE 8.11 The smooth ER (SER). Electron micrograph of a Leydig cell from the
testis showin...
FIGURE 8.12 Polarized structure of a secretory cell. (a) Drawing of a mucus-
secreting goblet...
FIGURE 8.13 A schematic model of the synthesis of a secretory protein (or a
lysosomal enzyme...
FIGURE 8.14 A schematic model for the synthesis of an integral membrane
protein that contain...
FIGURE 8.15 Maintenance of membrane asymmetry. As each protein is
synthesized in the RER, it...
FIGURE 8.16 Modifying the lipid composition of membranes. (a) Histogram
indicating the perce...
FIGURE 8.17 Steps in the synthesis of the core portion of an N-linked
oligosaccharide in the...
FIGURE 8.18 Quality control: ensuring that misfolded proteins do not proceed
forward. Based ...
FIGURE 8.19 A model of the mammalian unfolded protein response (UPR). The
ER contains transm...
FIGURE 8.20 Visualizing membrane traffic with the use of a fluorescent tag. This
series of p...
FIGURE 8.21 The Golgi complex. (a) Schematic model of a portion of a Golgi
complex from an e...
FIGURE 8.22 Regional differences in membrane composition across the Golgi
stack. (a) Reduced...
FIGURE 8.23 Steps in the glycosylation of a typical mammalian N-linked
oligosaccharide in th...
FIGURE 8.24 The dynamics of transport through the Golgi complex. (a) In the
vesicular transp...
FIGURE 8.25 Coated vesicles. These electron micrographs show the membranes of
these vesicles...
FIGURE 8.26 Proposed movement of materials by vesicular transport between
membranous compart...
FIGURE 8.27 Proposed roles of the COPII coat proteins in generating membrane
curvature, asse...
FIGURE 8.28 Structure of vesicle coats. (a) Molecular model of the outer Sec13–
Sec31 cage of...
FIGURE 8.29 Retrieving ER proteins. Resident proteins of the ER contain amino
acid sequences...
FIGURE 8.30 Targeting lysosomal enzymes to lysosomes. (a) Lysosomal enzymes
are recognized b...
FIGURE 8.31 The formation of clathrin-coated vesicles at the TGN. Clathrin-
coated vesicles t...
FIGURE 1 Lysosomal storage disorders. Electron micrograph of a section through
a portion ...
FIGURE 8.32 Proposed steps in the targeting of transport vesicles to target
membranes. (a) A...
FIGURE 8.33 A model of the interactions between v- and t-SNAREs leading to
membrane fusion a...
FIGURE 8.34 Illustration of extracellular vesicles. Extracellular vesicles can vary
in size ...
FIGURE 8.35 Lysosomes. Portion of a phagocytic Kupffer cell of the liver showing
at least 10...
FIGURE 8.36 Autophagy. Electron micrograph of a mitochondrion and
peroxisome enclosed in a d...
FIGURE 8.37 A summary of the autophagic pathway. The steps are described in
the text....
FIGURE 8.38 Plant cell vacuoles. (a) Each of the cylindrical leaf cells of the
aquatic plant...
FIGURE 8.39 Receptor-mediated endocytosis. This sequence of micrographs
shows the steps in t...
FIGURE 8.40 Coated pits. (a) Electron micrograph of a replica formed on the
extracellular su...
FIGURE 8.41 Clathrin triskelions. Electron micrograph of a metal-shadowed
preparation of cla...
FIGURE 8.42 Molecular organization of a coated vesicle. (a) Schematic drawing of
the surface...
FIGURE 8.43 The role of dynamin in the formation of clathrin-coated vesicles. (a)
The clathr...
FIGURE 8.44 A structural model depicting the changes in protein conformation
that occur upon...
FIGURE 1 (a) A handmade model of an “empty basket” that would form the surface
lattice of...
FIGURE 2 HMG CoA reductase activity in normal fibroblasts was measured
following addition...
FIGURE 3 Fibroblast cells from either a control subject (closed circles) or a patient
wit...
 FIGURE 4 Time course of radioactive [125I]-labeled LDL binding to cells from a
normal sub...
FIGURE 5 Electron micrograph showing the binding of LDL to a coated pit of a
human fibrob...
FIGURE 6 A series of fluorescence images showing the capture of a single red-
fluorescent ...
FIGURE 8.45 The endocytic pathway. (a) The movement of materials from the
extracellular spac...
FIGURE 8.46 LDL cholesterol. Each particle consists of esterified cholesterol
molecules, sur...
FIGURE 8.47 A model of atherosclerotic plaque formation. According to this
model, plaque for...
FIGURE 8.48 Phagocytosis. (a) The process of engulfment as illustrated by a
polymorphonuclea...
FIGURE 8.49 Importing proteins into a mitochondrion. (a) Proposed steps taken
by proteins im...
FIGURE 8.50 Importing proteins into a chloroplast. Proteins encoded by nuclear
genes are syn...
CHAPTER 9
FIGURE 9.1 An overview of the structure and functions of the cytoskeleton.
Schematic drawin...
FIGURE 9.2 An example of the role of microtubules in transporting organelles.
The peroxisom...
FIGURE 9.3 The structure of microtubules. (a) Electron micrograph of negatively
stained mic...
FIGURE 9.4 Microtubule Associated Proteins (MAPs). Structure of several
important MAPs dete...
FIGURE 9.5 Localization of microtubules. The localization of microtubules of a
flattened, c...
FIGURE 9.6 Visualization of cellulose synthase demonstrates functional
association with mic...
FIGURE 9.7 Axonal transport. (a) Schematic drawing of a nerve cell showing the
movement of...
FIGURE 9.8 Visualizing axonal transport. (a–c) These video micrographs show the
progression...
FIGURE 9.9 Mutations affecting microtubules can cause spiral growth in
Arabidopsis. (Top ro...
FIGURE 9.10 Longitudinal expansion of cells with parallel microfibril bands
results in strai...
FIGURE 9.11 Kinesin. (a) Structure of a kinesin-1 molecule, which consists of two
heavy chai...
FIGURE 1 Single steps of kinesin as it walks along the microtubule. Displacement
from the...
FIGURE 9.12 Alteration in the phenotype of a cell lacking a member of the kinesin
superfamil...
FIGURE 9.13 Cytoplasmic dynein and organelle transport by microtubule-tracking
motor protein...
FIGURE 9.14 The centrosome. (a) Schematic diagram of a centrosome showing
the paired centrio...
FIGURE 9.15 Microtubule nucleation at the centrosome. (a) Human MKN-1 cells
were treated wit...
FIGURE 9.16 The role of γ-tubulin in centrosome function. (a) Image shows a
mitotic spindle...
FIGURE 9.17 Four major arrays of microtubules present during the cell cycle of a
plant cell....
FIGURE 9.18 Nucleation of plant cortical microtubules. (a) The micrographs show
a portion of...
FIGURE 9.19 Microtubules assembled in the test tube. Electron micrograph of
frozen, unfixed...
FIGURE 9.20 The assembly of tubulin onto an existing microtubular structure.
Electron microg...
FIGURE 9.21 The structural cap model of dynamic instability. According to the
model, the gro...
FIGURE 9.22 Microtubule dynamics in living cells. This cultured fibroblast was
injected with...
FIGURE 9.23 Dynamic instability. This series of photographs shows the changes
in length of a...
FIGURE 9.24 Binding of a microtubule plus-end tracking protein (+TIP) The
micrograph shows a...
FIGURE 9.25 Cilia in the human body. (a) Immunofluorescence image showing a
single primary c...
FIGURE 9.26 Ciliary beat. (a) The various stages in the beat of a cilium. (b) The
cilia on t...
FIGURE 9.27 Eukaryotic flagella. (a) The unicellular alga Chlamydomonas
reinhardtii. Unlike...
FIGURE 9.28 The structure of a ciliary or flagellar axoneme. (a) Cross section
through a spe...
FIGURE 9.29 Longitudinal view of an axoneme. (a) Electron micrograph of a
median longitudina...
FIGURE 1 Defective primary cilia in the kidney lead to polycystic kidney disease.
Image s...
FIGURE 9.30 Basal bodies and axonemes. (a) Electron micrograph of a
longitudinal section thr...
FIGURE 9.31 Intraflagellar transport (IFT). Electron micrograph of a longitudinal
section of...
FIGURE 9.32 A model of the structure and function of flagellar/ciliary dynein. (a)
Platinum...
FIGURE 9.33 Schematic representation of the forces that drive ciliary or flagellar
motility....
FIGURE 9.34 The sliding microtubule mechanism of ciliary or flagellar motility.
Schematic di...
FIGURE 9.35 Cytoskeletal elements are connected to one another by protein
cross-bridges. Ele...
FIGURE 9.36 A model of intermediate filament assembly and architecture. (a)
Each monomer has...
FIGURE 9.37 Experimental demonstration of the dynamic character of
intermediate filaments. T...
FIGURE 9.38 The organization of intermediate filaments (IFs) within an epithelial
cell. (a)...
FIGURE 9.39 Actin filament structure. (a) Three-dimensional structure of an actin
filament....
FIGURE 9.40 Determining the location and polarity of actin filaments using the S1
subunit of...
FIGURE 9.41 Actin assembly in vitro. (a) Electron micrograph of a short actin
filament that...
FIGURE 9.42 Experimental demonstration of a role for myosin II in the
directional movement o...
FIGURE 9.43 Structure of a myosin II molecule. (a) Electron micrograph of
negatively stained...
FIGURE 9.44 In vitro motility assay for myosin. (a) Schematic drawing in which
myosin heads...
FIGURE 9.45 Structure of a bipolar myosin II filament. (a) Schematic diagram of
the staggere...
FIGURE 9.46 Myosin V—a two-headed unconventional myosin involved in
organelle transport. (a)...
FIGURE 9.47 The contrasting roles of microtubule- and microfilament-based
motors in intracel...
FIGURE 9.48 Hair cells, actin bundles, and unconventional myosins. (a) Drawing
of a hair cel...
FIGURE 9.49 The structure of skeletal muscle. (a) Levels of organization of a
skeletal muscl...
FIGURE 9.50 The contractile machinery of a sarcomere. (a) Diagram of a
sarcomere showing the...
FIGURE 9.51 The shortening of the sarcomere during muscle contraction. (a)
Schematic diagram...
FIGURE 9.52 The molecular organization of the thin filaments. Each thin filament
consists of...
FIGURE 9.53 The arrangement of titin molecules within the sarcomere. These
huge elastic mole...
FIGURE 9.54 Model of the swinging lever arm of a myosin II molecule. (a) During
the power st...
FIGURE 9.55 A schematic model of the actinomyosin contractile cycle. The
movement of the thi...
FIGURE 9.56 The functional anatomy of a muscle fiber. Calcium is housed in the
elaborate net...
FIGURE 9.57 The role of tropomyosin in muscle contraction. Schematic diagram
of how the myos...
FIGURE 9.58 Understanding the length–tension relation for muscle in terms of
sarcomere struc...
FIGURE 9.59 Different arrangements of actin filaments within a cell. These
electron microgra...
FIGURE 9.60 The roles of actin-binding proteins.
FIGURE 9.61 Actin filaments and actin-binding proteins in a microvillus.
Microvilli are pres...
FIGURE 9.62 Scanning electron micrograph of a mouse fibroblast crawling over
the surface of...
FIGURE 9.63 The repetitive sequence of activities that occur as a cell crawls over
the subst...
FIGURE 9.64 The leading edge of a motile cell. (a) The leading edge of this motile
fibroblas...
FIGURE 9.65 Directed cell motility. (a) Micrograph of a white blood cell (a
neutrophil) that...
FIGURE 1 Cell motility can be driven by actin polymerization. (a) Fluorescence
micrograph...
FIGURE 2 Still image from a computational simulation of actin-based motility of a
Listeria...
FIGURE 9.66 The structural basis of lamellipodial extension. Electron micrograph
of a replic...
FIGURE 9.67 Distribution of traction forces within a migrating fibroblast. (a) As a
 cell mig...
FIGURE 9.68 The roles of actin and myosin in the lamellipodial-based movement
of fish kerato...
FIGURE 9.69 The structure of a growth cone: the motile tip of a growing axon. (a)
A video im...
FIGURE 9.70 The directed movements of a growth cone. (a) A video image of a
live growth cone...
FIGURE 9.71 Early stages in the development of the vertebrate nervous system.
(a–d) Schemati...
FIGURE 9.72 Bacterial cytoskeletal filaments carry out functions similar to their
eukaryotic...
FIGURE 9.73 ParM segregates low-copy number plasmids. Still image from an
animation demonstr...
CHAPTER 10
FIGURE 10.1 An overview depicting several of the most important early
discoveries on the nat...
FIGURE 10.2 Events occurring in the roundworm Ascaris following fertilization,
as reported i...
FIGURE 10.3 Homologous chromosomes. Sutton’s drawing of the homologous
chromosomes of the ma...
FIGURE 10.4 The fruit fly Drosophila melanogaster. Photograph of a wild-type
female fruit fl...
FIGURE 10.5 Fruit flies have four pairs of homologous chromosomes, one of
which is very smal...
FIGURE 10.6 Visualizing sites of crossing over. Homologous chromosomes wrap
around each othe...
FIGURE 10.7 Crossing over provides the mechanism for reshuffling alleles
between maternal an...
FIGURE 10.8 Giant polytene chromosomes of larval insects. (a) These giant
polytene chromosom...
FIGURE 1 The large glistening colonies on the right are virulent S-type
pneumococci, wher...
FIGURE 2 Outline of the experiment by Griffith of the discovery of bacterial
transformati...
FIGURE 3 Electron micrograph of a bacterial cell infected by T4 bacteriophage.
Each phage...
FIGURE 4 The Hershey–Chase experiment. (a) Bacterial cells infected with phage
containing....
FIGURE 10.9 Model of DNA built by James Watson and Francis Crick at
Cambridge University, 19...
FIGURE 10.10 The chemical structure of DNA. (a) Model of a DNA nucleotide
containing the base...
FIGURE 10.11 The double helix. (a) Schematic representation of the DNA double
helix. (b) Spac...
FIGURE 10.12 Three functions required of the genetic material. (a) DNA must
contain the infor...
FIGURE 10.13 Supercoiled DNA. (a,b) Electron micrographs showing the
differences in conformat...
FIGURE 10.14 Underwound DNA. The DNA molecule on the left is underwound;
that is, it has more...
FIGURE 10.15 DNA topoisomerases. (a) A model depicting the action of human
topoisomerase I. T...
FIGURE 10.16 Thermal denaturation of DNA. A thermal denaturation curve for
native bacteriopha...
FIGURE 10.17 The kinetics of renaturation of viral and bacterial DNAs. The curves
show the re...
FIGURE 10.18 An idealized plot showing the kinetics of renaturation of eukaryotic
DNA. When s...
FIGURE 10.19 DNA fingerprinting. In this technique, which is used widely to
identify an indiv...
FIGURE 1 Trinucleotide repeat sequences and human disease. The top line shows a
generaliz...
FIGURE 10.20 Fluorescence in situ hybridization and the localization of satellite
DNA. (a) Th...
FIGURE 10.21 Chromosomal localization of a nonrepeated DNA sequence. These
mitotic chromosome...
FIGURE 10.22 A sampling of agricultural crops that are polyploid. Pictured are oil
from oilse...
FIGURE 10.23 Unequal crossing over between duplicated genes provides a
mechanism for generati...
FIGURE 10.24 A pathway for the evolution of globin genes. Exons are shown in
green, introns i...
FIGURE 10.25 Visible manifestations of transposition in maize. Kernels of corn
are typically ...
FIGURE 10.26 Transposition of a bacterial transposon by a “cut-and-paste”
mechanism. As discu...
FIGURE 10.27 Schematic pathways in the movement of transposable elements. (a)
DNA transposons...
FIGURE 10.28 Genome comparisons. Among eukaryotes with genomes that have
been sequenced, the ...
 FIGURE 10.29 Duplication of the amylase gene during human evolution. In the
results depicted ...
FIGURE 1 The genome is divided into blocks (haplotypes). The top line shows a
hypothetica...
FIGURE 10.30 Structural variants. (a) Schematic representation of the major
types of genomic ...
FIGURE 10.31 Photograph of mango tree with a crown gall tumor, likely caused by
Agrobacterium...
CHAPTER 11
FIGURE 11.1 The Beadle–Tatum experiment for the isolation of genetic mutants in
Neurospora. ...
FIGURE 11.2 An overview of the flow of information in a eukaryotic cell. The DNA
of the chro...
FIGURE 11.3 Two-dimensional structure of a bacterial ribosomal RNA showing
the extensive bas...
FIGURE 11.4 Chain elongation during transcription. (a) A schematic model of the
elongation o...
FIGURE 11.5 Examples of experimental techniques to follow the activities of single
RNA polym...
FIGURE 11.6 Schematic representation of the initiation of transcription in
bacteria. (a) In ...
FIGURE 11.7 The basic elements of a promoter region in the DNA of the bacterium
E. coli. The...
FIGURE 11.8 A comparison of prokaryotic and eukaryotic RNA polymerase
structure. (a) RNA pol...
FIGURE 11.9 The macromolecular composition of a mammalian ribosome. This
schematic drawing s...
FIGURE 11.10 The nucleolus. (a) Light micrograph of human lung fibroblast cells
stained with ...
FIGURE 11.11 Kinetic analysis of rRNA synthesis and processing. A culture of
mammalian cells ...
FIGURE 11.12 A proposed scheme for the processing of mammalian ribosomal
RNA. The primary tra...
FIGURE 11.13 Modifying the pre-rRNA. (a) The most frequent modifications to
nucleotides in a ...
FIGURE 11.14 The arrangement of genes that code for transfer RNAs in Xenopus.
A 3.18-kilobase...
FIGURE 11.15 The formation of heterogeneous nuclear RNA (hnRNA) and its
conversion into small...
FIGURE 11.16 Initiation of transcription from a eukaryotic polymerase II
promoter. (a) Nucleo...
FIGURE 11.17 Structure of the preinitiation complex determined by cryo-EM. RNA
polymerase II ...
FIGURE 11.18 Initiation of transcription by RNA polymerase II is associated with
phosphorylat...
FIGURE 11.19 Structure of the human β-globin mRNA. The mRNA contains a 5′
methylguanosine cap...
FIGURE 11.20 The difference in size between hnRNAs and mRNAs. Electron
micrographs of metal-s...
FIGURE 11.21 The discovery of intervening sequences (introns). A portion of the
adenovirus ge...
FIGURE 11.22 The discovery of introns in a eukaryotic gene. As discussed in
Chapter 18, bacte...
FIGURE 11.23 Visualizing an intron in the globin gene. Electron micrographs of
hybrids formed...
FIGURE 11.24 Visualizing introns in the ovalbumin gene. Electron micrograph of
a hybrid forme...
FIGURE 11.25 Pre-mRNA transcripts are processed as they are synthesized (i.e.,
cotranscriptio...
FIGURE 11.26 Steps in the addition of a 5′ methylguanosine cap and a 3′ poly(A)
tail to a pre...
FIGURE 11.27 Overview of the steps during the processing of the globin mRNA.
Introns are show...
FIGURE 11.28 Nucleotide sequences at the splice sites of pre-mRNAs. In addition
to encoding t...
FIGURE 11.29 The structure and self-splicing pathway of group II introns. (a)
Two-dimensional...
FIGURE 11.30 Schematic model of the assembly of the splicing machinery and
some of the steps ...
FIGURE 11.31 The structure of an snRNP. Model of a U1 snRNP particle based on
biochemical dat...
FIGURE 11.32 Schematic representation of a mechanism for the coordination of
transcription, c...
FIGURE 11.33 Processing the ovomucoid pre-mRNA. The photograph shows a
Northern blot, a techn...
FIGURE 11.34 RNA interference. (a) Petunia plants normally have purple flowers.
The flowers o...
FIGURE 11.35 The formation and mechanism of action of siRNAs and miRNAs.
(a) In step 1, both ...
FIGURE 1 RNAi leads to reduced TTR protein deposition in nervous tissue of the
dorsal roo...
FIGURE 11.36 MicroRNAs are synthesized in specific tissues during embryonic
development. Thes...
FIGURE 11.37 The distinction between an overlapping and a nonoverlapping
genetic code. The ef...
FIGURE 11.38 The genetic code. This universal decoder chart lists each of the 64
possible mRN...
FIGURE 11.39 Genes can be subject to several types of mutations. Red lines
denote codons. (a)...
FIGURE 11.40 Two-dimensional structure of transfer RNAs. (a) The nucleotide
sequence of the c...
FIGURE 11.41 The structure of a tRNA. (a) Two-dimensional structure of a yeast
phenylalanyl-t...
FIGURE 11.42 The wobble in the interaction between codons and anticodons. In
some cases, the ...
FIGURE 11.43 Three-dimensional portrait of the interaction between a tRNA and
its aminoacyl-t...
FIGURE 11.44 Initiation of protein synthesis in bacteria. In step 1, initiation of
translatio...
FIGURE 11.45 Initiation of protein synthesis in eukaryotes. As discussed in the
text, initiat...
FIGURE 11.46 Model of the bacterial ribosome based on X-ray crystallographic
data, showing tR...
FIGURE 11.47 Schematic representation of the steps in elongation during
translation in bacter...
FIGURE 11.48 Structural model of the stages of translocation during translational
elongation ...
FIGURE 1 Purified 32P-labeled Tetrahymena ribosomal RNA, transcribed at
different (NH4)2S...
FIGURE 2 The results of polyacrylamide gel electrophoresis of reaction mixtures
that had ...
FIGURE 3 A molecular model of a portion of the catalytic RNA subunit of bacterial
ribonuc...
FIGURE 11.49 Structural model of the first step of translational termination in
bacteria. Whe...
FIGURE 11.50 Polyribosomes. (a) Schematic drawing of a polyribosome
(polysome). (b) This thre...
FIGURE 11.51 Visualizing transcription and translation. Electron micrograph of
portions of an...
 FIGURE 11.52 DNA origami methodology. A long DNA scaffold (usually derived
from a bacteriopha...
FIGURE 11.53 Some of the shapes that have been built using DNA origami. Top
row shows compute...
CHAPTER 12
FIGURE 12.1 Kinetics of β-galactosidase induction in E. coli. When a β-galactoside
such as l...
FIGURE 12.2 Organization of a bacterial operon. The enzymes that make up a
metabolic pathway...
FIGURE 12.3 Gene regulation by operons. Inducible and repressible operons work
on a similar ...
FIGURE 12.4 Nucleotide sequence of the control regions of the lac operon. The
binding site f...
FIGURE 12.5 Computer-aided design of digital logic circuits based on
transcriptional control...
FIGURE 12.6 The cell nucleus. (a) Electron micrograph of an interphase HeLa cell
nucleus. He..
FIGURE 12.7 The nuclear envelope. (a) Schematic drawing showing the double
membrane, nuclear...
FIGURE 12.8 The nuclear lamina. (a) Nucleus of a cultured human cell that has
been stained w...
FIGURE 12.9 The movement of materials through the nuclear pore. (a) Electron
micrograph of t...
FIGURE 12.10 Scanning electron micrographs of the nuclear pore complex from
isolated nuclear ...
FIGURE 12.11 A model of a vertebrate nuclear pore complex (NPC). (a) Schematic
representation...
FIGURE 12.12 Importing proteins from the cytoplasm into the nucleus. (a)
Proposed steps in nu...
FIGURE 12.13 Nucleosomal organization of chromatin. (a) Schematic diagram
showing the structu...
FIGURE 12.14 The structure of a nucleosome. (a) Schematic representation of a
nucleosome core...
FIGURE 12.15 The 30-nm fiber. (a) Electron micrograph of a 30-nm chromatin
fiber released fro...
FIGURE 12.16 Chromatin loops: a higher level of chromatin structure. (a) Electron
micrograph ...
FIGURE 12.17 Levels of organization of chromatin. Naked DNA molecules are
wrapped around hist...
FIGURE 12.18 Facultative heterochromatin: the inactive X chromosome. (a) The
inactivated X ch...
FIGURE 12.19 Histone modifications and the histone code. The amino terminal
tails from histon...
FIGURE 12.20 Examples of proteins that bind selectively to modified H3 or H4
residues. Each o...
FIGURE 12.21 Experimental demonstration of a correlation between
transcriptional activity and...
FIGURE 12.22 A model in which small RNAs govern the formation of
heterochromatin. In this mod...
FIGURE 12.23 Human mitotic chromosomes and karyotypes. (a) Procedure used
to obtain preparati...
FIGURE 1 The effect of inversion. Crossing over between a normal chromosome
(purple) and ...
FIGURE 2 A translocation. Micrograph shows a set of human chromosomes in
which chromosome...
FIGURE 3 Translocation and evolution. If the only two ape chromosomes that have
no counte...
FIGURE 12.24 Telomeres. (a) In situ hybridization of a DNA probe containing the
sequence TTAG...
FIGURE 12.25 The end-replication problem and the role of telomerase. (a) When
the DNA of a ch...
FIGURE 12.26 Telomerase and chromosome integrity. The chromosomes in this
micrograph are from...
FIGURE 12.27 Each mitotic chromosome has a centromere with a site marked by a
distinct indent...
FIGURE 12.28 Chromosome territories. (a) Three and (b) all 23 pairs of human
chromosomes were...
FIGURE 12.29 Localizing specific chromosomes within an interphase nucleus.
Micrograph of the ...
FIGURE 12.30 Interactions can occur between distantly located genes in response
to physiologi...
FIGURE 12.31 Global packing of the genome within the nucleus. By combining
measurements of ch...
FIGURE 12.32 Nuclear compartmentalization of the cell’s mRNA processing
machinery. (a) The nu...
FIGURE 12.33 The cloning of animals demonstrates that nuclei retain a complete
complement of ...
FIGURE 12.34 Eukaryotic gene regulation. Transcriptional control mechanisms
operate by determ...
FIGURE 12.35 Experimental demonstration of tissue-specific gene expression.
Transcription of ...
FIGURE 12.36 DNA microarrays and analysis of gene expression. (a) Steps in the
construction o...
FIGURE 12.37 Transcription profiling to personalize breast cancer therapy.
Microarrays and RN...
FIGURE 12.38 Combinatorial control of transcription. Transcription of the Oct4
gene requires ...
FIGURE 12.39 Interactions between transcription factors bound to different sites
in the regul...
FIGURE 12.40 Phenotypic conversion induced by abnormal expression of a single
transcription f...
FIGURE 12.41 Interaction between a transcription factor and its DNA target
sequence. A model ...
FIGURE 12.42 Zinc-finger transcription factors. (a) Structure of the complex
between a protei...
FIGURE 12.43 Basic helix–loop–helix (bHLH) transcription factors. (a) MyoD, a
dimeric transcr...
FIGURE 12.44 Modifying the DNA-binding specificities of transcription factors
through dimeriz...
FIGURE 12.45 Regulating transcription from the rat PEPCK gene. Transcription
of this gene, li...
FIGURE 12.46 Identifying promoter sequences required for transcription. The top
line shows th...
FIGURE 12.47 Use of chromatin immunoprecipitation (ChIP) to identify
transcription-factor bin...
FIGURE 12.48 Activation of a gene by a steroid hormone. The hormone cortisol, a
glucocorticoi...
FIGURE 12.49 The mechanisms by which transcriptional activators bound at
distant sites can in...
FIGURE 12.50 Histone modifications can act as signatures of transcribed
chromatin regions. Th...
FIGURE 12.51 A model describing the activation of transcription. Transcription
factors, such ...
FIGURE 12.52 Chromatin remodeling. In pathway 1, a key nucleosome slides
along the DNA, expos...
FIGURE 12.53 The nucleosomal landscape of yeast genes. The top portion of the
illustration sh...
FIGURE 12.54 A model for transcriptional repression. Histone tails in the
promoter regions of ...
FIGURE 12.55 Changes in DNA methylation levels during mammalian
 development. The DNA of the f...
FIGURE 12.56 An lncRNA acting as a mediator of transcriptional repression. In
step 1, the lnc...
FIGURE 12.57 Diagram of the ABC system of transcription factors regulating
flower development...
FIGURE 12.58 Alternative splicing of the fibronectin gene. The fibronectin gene
consists of a...
FIGURE 12.59 A more complex example of alternative splicing. Most eukaryotic
genes are subjec...
FIGURE 12.60 Mechanisms of alternative splicing. (a) Changes in the sequence of
a 5′ splice s...
FIGURE 12.61 A model for the mechanism of translational activation of mRNAs
following fertili...
FIGURE 12.62 5′ UTR control of ferritin mRNA translation. When iron
concentrations are low, a...
FIGURE 12.63 Cytoplasmic localization of mRNAs. (a) Schematic drawings
showing three stages i...
FIGURE 12.64 mRNA degradation in mammalian cells. (a, b) The steps depicted
in these drawings...
FIGURE 12.65 miRNA mediated gene silencing. miRNAs, as part of an miRNP
protein complex as il...
FIGURE 12.66 Proteasome structure and function. (a) High-resolution cryo-EM
structure of the ...
CHAPTER 13
FIGURE 13.1 The original Watson–Crick proposal for the replication of a double-
helical molec...
FIGURE 13.2 Three alternate schemes of replication. Semiconservative replication
is depicted...
FIGURE 13.3 Experiment demonstrating that DNA replication in bacteria is
semiconservative. D...
FIGURE 13.4 Experimental demonstration that DNA replication occurs
semiconservatively in euk...
FIGURE 13.5 Model of a circular bacterial chromosome undergoing bidirectional,
semiconservat...
FIGURE 13.6 The unwinding problem. (a) The effect of unwinding a two-stranded
rope that has ...
FIGURE 13.7 Templates and nontemplates for DNA polymerase activity. (a)
Examples of DNA stru...
FIGURE 13.8 The activity of a DNA polymerase. (a) The polymerization of a
nucleotide onto th...
FIGURE 13.9 The two strands of a double helix are synthesized by different
sequences of even...
FIGURE 13.10 Results of an experiment showing that part of the DNA is
synthesized as small fr...
FIGURE 13.11 The use of short RNA fragments as removable primers in initiating
synthesis of e...
FIGURE 13.12 The roles of the DNA helicase, single-stranded DNA-binding
proteins, and primase...
FIGURE 13.13 Replication of the leading and lagging strands in E. coli is
accomplished by two...
FIGURE 13.14 Schematic representation of DNA polymerase III holoenzyme. The
holoenzyme contai...
FIGURE 13.15 The β sliding clamp and clamp loader. (a) Space-filling model
showing the two su...
FIGURE 13.16 The exonuclease activities of DNA polymerase I. (a) The 5′ → 3′
exonuclease func...
FIGURE 13.17 Geometry of proper (top row) and mismatched (bottom row) base
pairs.
FIGURE 13.18 Activation of the 3′ → 5′ exonuclease of DNA polymerase I. (a) A
schematic model...
FIGURE 13.19 Fully automated device for DNA storage invented by researchers at
Microsoft and ...
FIGURE 13.20 Experimental demonstration that replication in eukaryotic
chromosomes begins at ...
FIGURE 13.21 Steps leading to the replication of a yeast replicon. Yeast origins of
replicati...
FIGURE 13.22 A schematic view of the major components at the eukaryotic
replication fork. (a)...
FIGURE 13.23 Demonstration that replication activities do not occur uniformly
throughout the ...
FIGURE 13.24 The distribution of histone core complexes to daughter strands
following replica...
FIGURE 13.25 A pyrimidine dimer that has formed within a DNA duplex following
UV irradiation....
FIGURE 13.26 Nucleotide excision repair. The following steps are depicted in the
drawing and ...
FIGURE 13.27 Base excision repair. The steps are described in the text. Other
pathways for BE...
FIGURE 13.28 Detecting damaged bases during BER. In step 1, a DNA glycosylase
(named hOGG1) i...
 FIGURE 13.29 Repairing double-strand breaks (DSBs) by nonhomologous end
joining (NHEJ). (a) I...
FIGURE 13.30 Aerial view of the gamma garden facility in Hitachiomiya, Japan.
The cobalt-60 s...
CHAPTER 14
FIGURE 14.1 An overview of the eukaryotic cell cycle. This diagram of the cell cycle
indicat...
FIGURE 14.2 Experimental results demonstrating that replication occurs during a
defined peri...
FIGURE 14.3 Experimental demonstration that cells contain factors that stimulate
entry into ...
FIGURE 14.4 Fluctuation of cyclin and MPF levels during the cell cycle. This
drawing depicts...
FIGURE 1 Change of activity of the maturation-promoting factor in the oocyte
cytoplasm of...
FIGURE 2 Cycling of MPF activity in fertilized Rana pipiens eggs. Y axis:
percentage of r...
FIGURE 3 Maturation-promoting activity of HeLa cell extracts during different
stages of t...
FIGURE 4 Correlation of the level of cyclin with the cell division cycle. A
suspension of...
FIGURE 5 Kinetics of Xenopus oocyte activation by progesterone and cyclin A
mRNA. Large, ...
FIGURE 14.5 A simplified model for cell cycle regulation in fission yeast. The cell
cycle is...
FIGURE 14.6 Progression through the fission yeast cell cycle requires the
phosphorylation an...
FIGURE 14.7 Experimental demonstration of subcellular localization during the
cell cycle. Mi...
FIGURE 14.8 Cyclin–Cdks in the mammalian cell cycle. (a) Combinations between
various cyclin...
FIGURE 14.9 Models for the mechanism of action of two DNA damage
checkpoints. ATM and ATR ar...
FIGURE 14.10 p27: A Cdk inhibitor that arrests cell cycle progression. (a) Three-
dimensional ...
FIGURE 14.11 The stages of mitosis in an animal cell (left drawings) and a plant
cell (right ...
FIGURE 14.12 Prophase nuclear morphology. Light optical section through two
mouse cell nuclei...
FIGURE 14.13 The mitotic chromosome. (a) Electron micrograph of a whole-
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"In that case," Herndon said. "I consider myself in your employ. I'm
ready to leave tonight. As soon as the conditions I state have been
fulfilled to my complete satisfaction, I will submit my body to the
hands of your surgeon."

CHAPTER III
He bound himself over to the surgeon later that afternoon, after
money to the amount of ten thousand, nine hundred thirty golden
stellors had been deposited to his name in the Royal Borlaam Bank
in Galaxy Square, and after he had seen the neuronic mesh that was
embedded in the bodies of Benjin, Oversk, Dorgel, and Razumod.
Greater assurance of good faith than this he could not demand; he
would have to risk the rest.
The surgeon's quarters were farther along the Avenue of Bronze, in
a dilapidated old house that had no doubt been built in Third Empire
days. The surgeon himself was a wiry fellow with a puckered ray-
slash across one cheek and a foreshortened left leg. A retired pirate-
vessel medic, Herndon realized. No one else would perform such an
operation unquestioningly. He hoped the man had skill.
The operation itself took an hour, during which time Herndon was
under total anesthesia. He woke to find the copper operating-dome
lifting off him. He felt no different, even though he knew a network of
metal had been blasted into his body on the submolecular level.
"Well? Is it finished?"
"It is," the surgeon said.
Herndon glanced at Benjin. The little man held a glinting metal object
on his palm. "This is the control, Herndon. Let me demonstrate."
His hand closed, and instantaneously Herndon felt a bright bolt of
pain shiver through the calf of his leg. A twitch of Benjin's finger and
an arrow of red heat lanced Herndon's shoulder. Another twitch and
a clammy hand seemed to squeeze his heart.
"Enough!" Herndon shouted. He realized he had signed away his
liberty forever, if Benjin chose to exert control. But it did not matter to
him. He had actually signed away his liberty the day he had vowed
to watch the death of the Seigneur Krellig.
Benjin reached into his tunic-pocket and drew forth a little leather
portfolio. "Your passport and other travelling necessities," he
explained.
"I have my own passport," Herndon said.
Benjin shook his head. "This is a better one. It comes with a visa to
Vyapore." To the surgeon he said, "How soon can he travel?"
"Tonight, if necessary."
"Good. Herndon, you'll leave tonight."

The ship was the Lord Nathiir, a magnificent super-liner bound on a

thousand light-year cruise to the Rim stars. Benjin had arranged for
Herndon to travel outward on a luxury liner without cost, as part of
the entourage of Lord and Lady Moaris. Oversk had obtained the job
for him—second steward to the noble couple, who were vacationing
on the Rim pleasure-planet of Molleccogg. Herndon had not objected
when he learned that he was to travel in the company of Lord—and
especially Lady—Moaris.
The ship was the greatest of the Borlaam luxury fleet. Even on Deck
C, in his steward's quarters, Herndon rated a full-grav room with
synthik drapery and built-in chromichron; he had never lived so well
even at his parents' home, and they had been among the first people
of Zonnigog at one time.
His duties called for him to pay court upon the nobles each evening,
so that they might seem more resplendent in comparison with the
other aristocrats travelling aboard. The Moarises had brought the
largest entourage with them, over a hundred people including valets,
stewards, cooks, and paid sycophants.
Alone in his room during the hour of blastoff, Herndon studied his
papers. A visa to Vyapore. So that was where the starstones came
from—! Vyapore, the jungle planet of the Rim, where civilization
barely had a toehold. No wonder the starstone trade was so difficult
to control.
When the ship was safely aloft and the stasis generators had caused
the translation into nullspace, Herndon dressed in the formal black-
and-red court garments of Lord Moaris' entourage. Then, making his
way up the broad companionway, he headed for the Grand Ballroom,
where Lord Moaris and his lady were holding court for the first night
of the voyage outward.
The ballroom was festooned with ropes of living light. A dancing bear
from Albireo XII cavorted clumsily near the entrance as Herndon
entered. Borlaamese in uniforms identical to his own stood watch at
the door, and nodded to him when he identified himself as Second
Steward.
He stood for a moment alone at the threshold of the ballroom,
watching the glittering display. The Lord Nathiir was the playground
of the wealthy, and a goodly number of Borlaam's wealthiest were
here, vying with the ranking nobles, the Moarises, for splendor.
Herndon felt a twinge of bitterness. His people were from beyond the
sea, but by rank and preference he belonged in the bright lights of
the ballroom, not standing here in the garment of a steward. He
moved forward.
The noble couple sat on raised thrones at the far end, presiding over
a dancing-area in which the grav had been turned down; the couples
drifted gracefully, like figures out of fable, feet touching the ground
only at intervals.
Herndon recognized Lord Moaris from the auction. A dour, short,
thick-bodied individual he was, resplendent in his court robes, with a
fierce little beard stained bright red after the current fashion. He sat
stiffly upright on his throne, gripping the armrests of the carven chair
as if he were afraid of floating off toward the ceiling. In the air before
him shimmered the barely perceptible haze of a neutralizer field
designed to protect him from the shots of a possible assassin.
By his side sat his Lady, supremely self-possessed and lovely.
Herndon was astonished by her youth. No doubt the nobles had
means of restoring lost freshness to a woman's face, but there was
no way of recreating the youthful bloom so convincingly. The Lady
Moaris could not have been more than twenty-three or twenty-five.
Her husband was several decades older. It was small wonder that he
guarded her so jealously.
She smiled in sweet content at the scene before her. Herndon, too,
smiled—at her beauty, and at the use to which he hoped to put it.
Her skin was soft pink; a wench of the bath Herndon had met
belowdecks had told him she bathed in the cream of the ying-apple
twice daily. Her eyes were wide-set and clear, her nose finely made,
her lips two red arching curves. She wore a dress studded with
emeralds; it flowed from her like light. It was open at the throat,
revealing a firm bosom and strong shoulders. She clutched a
diamond-crusted scepter in one small hand.
Herndon looked around, found a lady of the court who was
unoccupied at the moment, and asked her to dance. They danced
silently, gliding in and out of the grav field; Herndon might have
found it a pleasant experience, but he was not primarily in search of
pleasant experiences now. He was concerned only with attracting
the attention of the Lady Moaris.
He was successful. It took time; but he was by far biggest and most
conspicuous man of the court assembled there, and it was
customary for Lord and Lady to leave their thrones, mingle with their
courtiers, even dance with them. Herndon danced with lady after
lady, until finally he found himself face to face with the Lady Moaris.
"Will you dance with me?" she asked. Her voice was like liquid
gossamer.
Herndon lowered himself in a courtly bow. "I would consider it the
greatest of honors, good Lady."
They danced. She was easy to hold; he sensed her warmness near
him, and he saw something in her eyes—a distant pinched look of
pain, perhaps—that told him all was not well between Lord and Lady.
She said, "I don't recognize you. What's your name?"
"Barr Herndon, milady. Of Zonnigog."
"Zonnigog, indeed! And why have you crossed ten thousand miles of
ocean to our city?"
Herndon smiled and gracefully dipped her through a whirling series
of pirouettes. "To seek fame and fortune, milady. Zonnigog is well
and good to live in, but the place to become known is the City of
Borlaam. For this reason I petitioned the Heitman Oversk to have me
added to the retinue of the Lord Moaris."
"You know Oversk, then? Well?"
"Not at all well. I served him a while; then I asked to move on."
"And so you go, climbing up and over your former masters, until you
scramble up the shoulders of the Lord Moaris to the feet of the
Seigneur. Is that the plan?"
She smiled disarmingly, drawing any possible malice from the words
she had uttered. Herndon nodded, saying in all sincerity, "I confess
this is my aim. Forgive me, though, for saying that there are reasons
that might cause me to remain in the service of the Lord Moaris
longer than I had originally intended."
A flush crossed her face. She understood. In a half-whisper she said.
"You are impertinent. I suppose it comes with good looks and a
strong body."
"Thank you, milady."
"I wasn't complimenting you," she said as the dance came to an end
and the musicians subsided. "I was criticizing. But what does it
matter? Thank you for the dance."
"May I have the pleasure of milady's company once again soon?"
Herndon asked.
"You may—but not too soon." She chuckled. "The Lord Moaris is
highly possessive. He resents it when I dance twice the same
evening with one member of the court."
Sadness darkened Herndon's face a moment. "Very well, then. But I
will go to Viewplate A and stare at the stars a while. If the Lady
seeks a companion, she will find one there."
She stared at him and flurried away without replying. But Herndon
felt a glow of inner satisfaction. The pieces were dropping into place.
The ladder was being constructed. Soon it would bring him to the
throneroom of the Seigneur Krellig. Beyond that he would need no
plans.

Viewplate A, on the uppermost deck of the vast liner, was reserved

for the first-class passengers and the members of their retinues. It
was an enormous room, shrouded at all times in darkness, at one
end of which a viewscreen opened out onto the glory of the heavens.
In nullspace, a hyperbolic section of space was visible at all times,
the stars in weird out-of-focus colors forming a breathtaking display.
Geometry went awry. A blazing panorama illuminated the room.
The first-class viewing-room was also known to be a trysting-place.
There, under cover of darkness, ladies might meet and make love to
cooks, lords to scullery-maids. An enterprising rogue with a nolight
camera might make a fortune taking a quick shot of such a room and
black-mailing his noble victims. But scanners at the door prevented
such devices from entering.
Herndon stood staring at the fiery gold and green of the closest stars
a while, his back to the door, until he heard a feminine voice whisper
to him.
"Barr Herndon?"
He turned. In the darkness it was difficult to tell who spoke; he saw a
girl about the height of the Lady Moaris, but in the dimness of the
illumination of the plate he could see it was not the Lady. This girl's
hair was dull red; the Lady's was golden. And he could see the pale
whiteness of this girl's breasts; the Lady's garment, while revealing,
had been somewhat more modest.
This was a lady of the court, then, perhaps enamoured of Herndon,
perhaps sent by the Lady Moaris as a test or as a messenger.
Herndon said, "I am he. What do you want?"
"I bring a message from—a noble lady," came the answering
whisper.
Smiling in the darkness Herndon said, "What does your mistress
have to say to me?"
"It cannot be spoken. Hold me in a close embrace as if we were
lovers, and I will give you what you need."
Shrugging, Herndon clasped the go-between in his arms with
feigned passion. Their lips met; their bodies pressed tight. Herndon
felt the girl's hand searching for his, and slipping something cool,
metallic into it. Her lips left his, travelled to his ear, and murmured:
"This is her key. Be there in half an hour."
They broke apart. Herndon nodded farewell to her and returned his
attention to the glories of the viewplate. He did not glance at the
object in his hand, but merely stored it in his pocket.
He counted out fifteen minutes in his mind, then left the viewing-
room and emerged on the main deck. The ball was still in progress,
but he learned from a guard on duty that the Lord and Lady Moaris
had already left for sleep, and that the festivities were soon to end.
Herndon slipped into a washroom and examined the key—for key it
was. It was a radionic opener, and imprinted on it were the numbers
1160.
His throat felt suddenly dry. The Lady Moaris was inviting him to her
room for the night—or was this a trap, and would Moaris and his
court be waiting for him, to gun him down and provide themselves
with some amusement? It was not beyond these nobles to arrange
such a thing.
But still—he remembered the clearness of her eyes, and the beauty
of her face. He could not believe she would be party to such a
scheme.
He waited out the remaining fifteen minutes. Then, moving
cautiously along the plush corridors, he found his way to Room 1160.
He listened a moment. Silence from within. His heart pounded
frantically, irking him; this was his first major test, possibly the
gateway to all his hopes, and it irritated him that he felt anxiety.
He touched the tip of the radionic opener to the door. The substance
of the door blurred as the energy barricade that composed it was
temporarily dissolved. Herndon stepped through quickly. Behind him,
the door returned to a state of solidity.
The light of the room was dim. The Lady Moaris awaited him,
wearing a gauzy dressing-gown. She smiled tensely at him; she
seemed ill-at-ease.
"Would I do otherwise?"
"I—wasn't sure. I'm not in the habit of doing things like this."
Herndon repressed a cynical smile. Such innocence was touching,
but highly improbable. He said nothing, and she went on: "I was
caught by your face—something harsh and terrible about it struck
me. I had to send for you, to know you better."
Ironically Herndon said, "I feel honored. I hadn't expected such an
invitation."
"You won't—think it's cheap of me, will you?" she said plaintively. It
was hardly the thing Herndon expected from the lips of the noble
Lady Moaris. But, as he stared at her slim body revealed beneath
the filmy robe, he understood that she might not be so noble after all
once the gaudy pretense was stripped away. He saw her as perhaps
she truly was: a young girl of great loveliness, married to a
domineering nobleman who valued her only for her use in public
display. It might explain this bedchamber summons to a Second
Steward.
He took her hand. "This is the height of my ambitions, milady.
Beyond this room, where can I go?"
But it was empty flattery he spoke. He darkened the room
illumination exultantly. With your conquest, Lady Moaris, he thought,
do I begin the conquest of the Seigneur Krellig!

CHAPTER IV

The voyage to Molleccogg lasted a week, absolute time aboard ship.

After their night together, Herndon had occasion to see the Lady
Moaris only twice more, and on both occasions she averted her eyes
from him, regarding him as if he were not there.
It was understandable. But Herndon held a promise from her that
she would see him again in three months' time, when she returned to
Borlaam; and she had further promised that she would use her
influence with her husband to have Herndon invited to the court of
the Seigneur.
The Lord Nathiir emerged from nullspace without difficulty and was
snared by the landing-field of Molleccogg Spacefield. Through the
viewing-screen on his own deck, Herndon saw the colorful splendor
of the pleasure-planet on which they were about to land, growing
larger now that they were in the final spiral.
But he did not intend to remain long on the world of Molleccogg.
He found the Chief Steward and applied for a leave of absence from
Lord Moaris' service, without pay.
"But you've just joined us," the Steward protested. "And now you
want to leave?"
"Only for a while," Herndon said. "I'll be back on Borlaam before any
of you are. I have business to attend to on another world in the Rim
area, and then I promise to return to Borlaam at my own expense to
rejoin the retinue of the Lord Moaris."
The Chief Steward grumbled and complained, but he could not find
anything particularly objectionable in Herndon's intentions, and so
finally he reluctantly granted the spacerogue permission to leave
Lord Moaris' service temporarily. Herndon packed his court costume
and clad himself in his old spacerogue garb; when the great liner
ultimately put down in Danzibool Harbor on Molleccogg, Herndon
was packed and ready, and he slipped off ship and into the thronged
confusion of the terminal.
Bollar Benjin and Heitman Oversk had instructed him most carefully
on what he was to do now. He pushed his way past a file of vile-
smelling lily-faced green Nnobonn and searched for a ticket-seller's
window. He found one, eventually, and produced the pre-paid travel
vouchers Benjin had given him.
"I want a one-way passage to Vyapore," he said to the flat-featured,
triple-eyed Guzmanno clerk who stared out from back of the wicker
screen.
"You need a visa to get to Vyapore," the clerk said. "These visas are
issued at infrequent intervals to certified personages. I don't see how
you—"
"I have a visa," Herndon snapped, and produced it. The clerk blinked
—one-two-three, in sequence—and his pale rose face flushed deep
cerise.
"So you do," he remarked at length. "It seems to be in order.
Passage will cost you eleven hundred sixty-five stellors of the
realm."
"I'll take a third-class ship," Herndon said. "I have a paid voucher for
such a voyage."
He handed it across. The clerk studied it for a long moment, then
said: "You have planned this very well. I accept the voucher. Here."
Herndon found himself holding one paid passage to Vyapore aboard
the freight-ship Zalasar.
The Zalasar turned out to be very little like the Lord Nathiir. It was an
old-fashioned unitube ship that rattled when it blasted off, shivered
when it translated to nullspace, and quivered all the week-long
journey from Molleccogg to Vyapore. It was indeed a third-class ship.
Its cargo was hardware: seventy-five thousand dry-strainers, eighty
thousand pressors, sixty thousand multiple fuse-screens, guarded by
a supercargo team of eight taciturn Ludvuri. Herndon was the only
human aboard. Humans did not often get visas to Vyapore.
They reached Vyapore seven days and a half after setting out from
Molleccogg. Ground temperature as they disembarked was well over
a hundred. Humidity was overpowering. Herndon knew about
Vyapore: it held perhaps five hundred humans, one spaceport,
infinite varieties of deadly local life, and several thousand non-
humans of all descriptions, some of them hiding, some of them doing
business, some of them searching for starstones.
Herndon had been well briefed. He knew who his contact was, and
he set about meeting him.

There was only one settled city on Vyapore, and because it was the
only one it was nameless. Herndon found a room in a cheap
boarding-house run by a swine-eared Dombruun, and washed the
sweat from his face with the unpleasantly acrid water of the tap.
Then he went downstairs into the bright noonday heat. The stench of
rotting vegetation drifted in from the surrounding jungle on a faint
breeze. Herndon said at the desk, "I'm looking for a Vonnimooro
named Mardlin. Is he around?"
"Over there," said the proprietor, pointing.
Mardlin the Vonnimooro was a small, weaselly-looking creature with
the protuberant snout, untrustworthy yellow eyes, and pebbly brown-
purple fur of his people. He looked up when Herndon approached.
When he spoke, it was in lingua spacia with a whistling, almost
obscene inflection.
"You looking for me?"
"It depends," Herndon said. "Are you Mardlin?"
The jackal-creature nodded. Herndon lowered himself to a nearby
seat and said in a quiet voice, "Bollar Benjin sent me to meet you.
Here are my credentials."
He tossed a milky-white clouded cube on the table between them.
Mardlin snatched it up hastily in his leathery claws and nudged the
activator. An image of Bollar Benjin appeared in the cloudy depths,
and a soft voice said, "Benjin speaking. The bearer of this cube is
known to me, and I trust him fully in all matters. You are to do the
same. He will accompany you to Borlaam with the consignment of
goods."
The voice died away and the image of Benjin vanished. The jackal
scowled. He muttered, "If Benjin sent a man to convey his goods,
why must I go?"
Herndon shrugged. "He wants both of us to make the trip, it seems.
What do you care? You're getting paid, aren't you?"
"And so are you," snapped Mardlin. "It isn't like Benjin to pay two
men to do the same job. And I don't like you, Rogue."
"Mutual," Herndon responded heartily. He stood up. "My orders say
I'm to take the freighter Dawnlight back to Borlaam tomorrow
evening. I'll meet you here one hour before to examine the
merchandise."

He made one other stop that day. It was a visit with Brennt, a
jewelmonger of Vyapore who served as the funnel between the
native starstone-miners and Benjin's courier, Mardlin.
Herndon gave his identifying cube to Brennt and said, once he had
satisfactorily proven himself, "I'd like to check your books on the last
consignment."
Brennt glanced up sharply. "We keep no books on starstones, idiot.
What do you want to know?"
Herndon frowned. "We suspect our courier of diverting some of our
stones to his own pocket. We have no way of checking up on him,
since we can't ask for vouchers of any kind in starstone traffic."
The Vyaporan shrugged. "All couriers steal."
"Starstones cost us eight thousand stellors apiece," Herndon said.
"We can't afford to lose any of them, at that price. Tell me how many
are being sent in the current shipment."
"I don't remember," Brennt said.
Scowling, Herndon said, "You and Mardlin are probably in league.
We have to take his word for what he brings us—but always, three or
four of the stones are defective. We believe he buys, say, forty
stones from you, pays the three hundred twenty thousand stellors
over to you from the account we provide, and then takes three or
four from the batch and replaces them with identical but defective
stones worth a hundred stellors or so apiece. The profit to him is
better than twenty thousand stellors a voyage.
"Or else," Herndon went on, "You deliberately sell him defective
stones at eight thousand stellors. But Mardlin's no fool, and neither
are we."
"What do you want to know?" the Vyaporan asked.
"How many functional starstones are included in the current
consignment?"
Sweat poured down Brennt's face. "Thirty-nine," he said after a long
pause.
"And did you also supply Mardlin with some blanks to substitute for
any of these thirty-nine?"
"N-no," Brennt said.
"Very good," said Herndon. He smiled. "I'm sorry to have seemed so
overbearing, but we had to find out this information. Will you accept
my apologies and shake?"
He held out his hand. Brennt eyed it uncertainly, then took it. With a
quick inward twitch Herndon jabbed a needle into the base of the
other's thumb. The quick-acting truth-drug took only seconds to
operate.
"Now," Herndon said, "the preliminaries are over. You understand the
details of our earlier conversation. Tell me, now: how many
starstones is Mardlin paying you for?"
Brennt's fleshless lips curled angrily, but he was defenseless against
the drug. "Thirty-nine," he said.
"At what total cost?"
"Three hundred twelve thousand stellors."
Herndon nodded. "How many of those thirty-nine are actually
functional starstones?"
"Thirty-five," Brennt said reluctantly.
"The other four are duds?"
"Yes."
"A sweet little racket. Did you supply Mardlin with the duds?"
"Yes. At two hundred stellors each."
"And what happens to the genuine stones that we pay for but that
never arrive on Borlaam?"
Brennt's eyes rolled despairingly. "Mardlin—Mardlin sells them to
someone else and pockets the money. I get five hundred stellors per
stone for keeping quiet."
"You've kept very quiet today," Herndon said. "Thanks very much for
the information, Brennt. I really should kill you—but you're much too
valuable to us for that. We'll let you live, but we're changing the
terms of our agreement. From now on we pay you only for actual
functioning starstones, not for an entire consignment. Do you like
that setup?"
"No," Brennt said.
"At least you speak truthfully now. But you're stuck with it. Mardlin is
no longer courier, by the way. We can't afford a man of his tastes in
our organization. I don't advise you try to make any deals with his
successor, whoever he is."
He turned and walked out of the shop.

Herndon knew that Brennt would probably notify Mardlin that the
game was up immediately, so the Vonnimooro could attempt to get
away. Herndon was not particularly worried about Mardlin escaping,
since he had a weapon that would work on the jackal-creature at any
distance whatever.
But he had sworn an oath to safeguard the combine's interests, and
Herndon was a man of his oath. Mardlin was in possession of thirty-
nine starstones for which the combine had paid. He did not want the
Vonnimooro to take those with him.
He legged it across town hurriedly to the house where the courier
lived while at the Vyapore end of his route. It took him fifteen minutes
from Brennt's to Mardlin's—more than enough time for a warning.
Mardlin's room was on the second story. Herndon drew his weapon
from his pocket and knocked.
"Mardlin?"
There was no answer. Herndon said, "I know you're in there, jackal.
The game's all over. You might as well open the door and let me in."
A needle came whistling through the door, embedded itself against
the opposite wall after missing Herndon's head by inches. Herndon
stepped out of range and glanced down at the object in his hand.
It was the master-control for the neuronic network installed in
Mardlin's body. It was quite carefully gradated; shifting the main
switch to six would leave the Vonnimooro in no condition to fire a
gun. Thoughtfully Herndon nudged the indicator up through the
degrees of pain to six and left it there.
He heard a thud within.
Putting his shoulder to the door, he cracked it open with one quick
heave. He stepped inside. Mardlin lay sprawled in the middle of the
floor, writhing in pain. Near him, but beyond his reach, lay the
needler he had dropped.
A suitcase sat open and half-filled on the bed. He had evidently
intended an immediate getaway.
"Shut ... that ... thing ... off ..." Mardlin muttered through pain-twisted
lips.
"First some information," Herndon said cheerfully. "I just had a talk
with Brennt. He says you've been doing some highly improper things
with our starstones. Is this true?"
Mardlin quivered on the floor but said nothing. Herndon raised the
control a quarter of a notch, intensifying the pain but not yet bringing
it to the killing range.
"Is this true?" he repeated.
"Yes—yes! Damn you, shut it off."
"At the time you had the network installed in your body, it was with
the understanding that you'd be loyal to the combine and so it would
never need to be used. But you took advantage of circumstances
and cheated us. Where's the current consignment of stones?"
"... suitcase lining," Mardlin muttered.
"Good," Herndon said. He scooped up the needler, pocketed it, and
shut off the master-control switch. The pain subsided in the
Vonnimooro's body, and he lay slumped, exhausted, too battered to
rise.
Efficiently Herndon ripped away the suitcase lining and found the
packet of starstones. He opened it. They were wrapped in shielding
tissue that protected any accidental viewer. He counted through
them; there were thirty-nine, as Brennt had said.
"Are any of these defective?" he asked.
Mardlin looked up from the floor with eyes yellow with pain and
hatred. "Look through them and see."
Instead of answering, Herndon shifted the control switch past six
again. Mardlin doubled up, clutching his head with clawlike hands.
"Yes! Yes! Six defectives!"
"Which means you sold six good ones for forty-eight thousand
stellors, less the three thousand you kicked back to Brennt to keep
quiet. So there should be forty-five thousand stellors here that you
owe us. Where are they?"
"Dresser drawer ... top...."
Herndon found the money, neatly stacked. A second time he shut off
the control device, and Mardlin relaxed.
"Okay," Herndon said. "I have the cash and I have the stones. But
there must be thousands of stellors that you've previously stolen
from us."
"You can have that too! Only don't turn that thing on again, please!"
Shrugging, Herndon said, "There isn't time for me to hunt down the
other money you stole from us. But we can ensure against your
doing it again."
He fulfilled the final part of Benjin's instructions by turning the control
switch to ten, the limit of sentient endurance. Every molecule of
Mardlin's wiry body felt unbearable pain; he screamed and danced
on the floor, but only for a moment. Nerve cells unable to handle the
overload of pain stimuli short-circuited. In seconds, his brain was
paralyzed. In less than a minute he was dead, though his tortured
limbs still quivered with convulsive post-mortuary jerks.
Herndon shut the device off. He had done his job. He felt neither
revulsion nor glee. All this was merely the preamble to what he
regarded as his ultimate destiny.
He gathered up jewels and money and walked out.
 CHAPTER V
A month later, he arrived on Borlaam via the freighter Dawnlight, as
scheduled, and passed through customs without difficulty despite the
fact that he was concealing more than three hundred thousand
stellors' worth of proscribed starstones on his person.
His first stop was the Avenue of Bronze, where he sought out Benjin
and the Heitman Oversk.
He explained crisply and briefly his activities since leaving Borlaam,
neglecting to mention the matter of the shipboard romance with the
Lady Moaris. While he spoke, both Benjin and Oversk stared eagerly
at him, and when he told of intimidating Brennt and killing the
treacherous Mardlin they beamed.
Herndon drew the packet of starstones from his cloak and laid them
on the wooden table. "There," he said. "The starstones. There were
some defectives, as you know, and I've brought back cash for them."
He added forty-five thousand stellors to the pile.
Benjin quickly caught up the money and the stones and said, "You've
done well, Herndon. Better than we expected. It was a lucky day
when you killed that proteus."
"Will you have more work for me?"
Oversk said, "Of course. You'll take Mardlin's place as the courier.
Didn't you realize that?"
Herndon had realized it, but it did not please him. He wanted to
remain on Borlaam, now that he had made himself known to the
Lady Moaris. He wanted to begin his climb toward Krellig. And if he
were to shuttle between Vyapore and Borlaam, the all-important
advantage he had attained would be lost.
But the Lady Moaris would not be back on Borlaam for nearly two
months. He could make one more round-trip for the combine without
seriously endangering his position. After that, he would have to find
some means of leaving their service. Of course, if they preferred to
keep him on they could compel him, but—
"When do I make the next trip?" he asked.
Benjin shrugged lazily. "Tomorrow, next week, next month—who
knows? We have plenty of stones on hand. There is no hurry for the
next trip. You can take a vacation now, while we sell these."
"No," Herndon said. "I want to leave immediately."
Oversk frowned at him. "Is there some reason for the urgency?"
"I don't want to stay on Borlaam just now," Herndon said. "There's no
need for me to explain further. It pleases me to make another trip to
Vyapore."
"He's eager," Benjin said. "It's a good sign."
"Mardlin was eager at first too," Oversk remarked balefully.
Herndon was out of his seat and at the nobleman's throat in an
instant. His needler grazed the skin of Oversk's adam's-apple.
"If you intend by that comparison to imply—"
Benjin tugged at Herndon's arm, "Sit down, rogue, and relax. The
Heitman is tired tonight, and the words slipped out. We trust you. Put
the needler away."
Reluctantly Herndon lowered the weapon. Oversk, white-faced
despite his tan, fingered his throat where Herndon's weapon had
touched it, but said nothing. Herndon regretted his hasty action, and
decided not to demand an apology. Oversk still could be useful to
him.
"A spacerogue's word is his bond," Herndon said. "I don't intend to
cheat you. When can I leave?"
"Tomorrow, if you wish," Benjin said. "We'll cable Brennt to have
another shipment ready for you."

This time he travelled to Vyapore aboard a transport freighter, since

there were no free tours with noblemen to be had at this season. He
reached the jungle world a little less than a month later. Brennt had
thirty-two jewels waiting for him. Thirty-two glittering little starstones,
each in its protective sheath, each longing to rob some man's mind
away with its beckoning dreams.
Herndon gathered them up and arranged a transfer of funds to the
amount of two hundred fifty-six thousand stellors. Brennt eyed him
bitterly throughout the whole transaction, but it was obvious that the
Vyaporan was in fear for his life, and would not dare attempt
duplicity. No word was said of Mardlin or his fate.
Bearing his precious burden, Herndon returned to Borlaam aboard a
second-class liner out of Diirhav, a neighboring world of some
considerable population. It was expensive, but he could not wait for
the next freight ship. By the time he returned to Borlaam the Lady
Moaris would have been back several weeks. He had promised the
Steward he would rejoin Moaris' service, and it was a promise he
intended to keep.
It had become winter when he reached Borlaam again with his
jewels. The daily sleet-rains sliced across the cities and the plains,
showering them with billions of icy knife-like particles. People
huddled together, waiting for the wintry cold to end.
Herndon made his way through streets clogged with snow that
glistened blue-white in the light of the glinting winter moon, and
delivered his gems to Oversk in the Avenue of Bronze. Benjin, he
learned, would be back shortly; he was engaged in an important
transaction.
Herndon warmed himself by the heat-wall and accepted cup after
cup of Oversk's costly Thrucian blue wine to ease his inner chill. The
commoner Dorgel entered after a while, followed by Marya and
Razumod, and together they examined the new shipment of
starstones Herndon had brought back, storing them with the rest of
their stock.
At length Benjin entered. The little man was almost numb with cold,
but his voice was warm as he said, "The deal is settled, Oversk! Oh
—Herndon—you're back, I see. Was it a good trip?"