Chapter 1

*Lecture PowerPoint
Major Themes of
Anatomy and
Physiology

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 Introduction
• Anatomy and physiology (A&P) is about human
structure and function—the biology of the human
body
• A&P is a foundation for advanced study in health
care, exercise physiology, pathophysiology, and
other health-care-related fields
• Considers the historical development and a
central concept of physiology—homeostasis

1-2
Anatomy—The Study of Form
• Examining structure of
the human body
– Inspection
– Palpation
– Auscultation
– Percussion
• Cadaver dissection
– Cutting and separation of
tissues to reveal their
relationships

• Comparative anatomy
Figure 1.1 – Study of more than one
species in order to examine
structural similarities and
differences, and analyze
evolutionary trends 1-3
 Anatomy—The Study of Form
• Exploratory surgery
– Open body and take a look inside
• Medical imaging
– Viewing the inside of the body without surgery
– Radiology—branch of medicine concerned with imaging
• Gross anatomy
– Study of structures that can be seen with the naked eye
• Cytology
– Study of structure and function of cells
• Histology (microscopic anatomy)
– Examination of cells with microscope
• Ultrastructure
– View molecular detail under electron microscope
• Histopathology
– Microscopic examination of tissues for signs of disease 1-4
 Physiology—The Study of Function

• Comparative physiology
– Limitations on human experimentation
– Study of different species to learn about bodily function
• Animal surgery
• Animal drug tests
– Basis for the development of new drugs and medical
procedures

1-5
The Birth of Modern Medicine
• Robert Hooke
– Made many improvements to
the compound microscope—
two lenses: ocular lens
(eyepiece) and objective lens
(near specimen)
• Invented specimen stage,
illuminator, coarse and fine
focus controls
• His microscopes magnified
only 30X
• First to see and name “cells”
– Published first
comprehensive book of
microscopy (Micrographia) in
Figure 1.4 1665
1-6
 The Birth of Modern Medicine
• Antony van Leeuwenhoek
– Invented a simple (single-lens) microscope with great
magnification to look at fabrics (200X)
– Published his observations of blood, lake water,
sperm, bacteria from tooth scrapings, and many other
things

1-7
 Cell Theory

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 The Birth of Modern Medicine

• Matthias Schleiden and Theodor Schwann

– With improved microscopes, examination of a wide
variety of specimens followed
– Concluded that “all organisms were composed of
cells”
– First tenet of cell theory
• Considered as the most important breakthrough in
biomedical history
• All functions of the body are interpreted as effects of
cellular activity

1-9
 Scientific Method
Testing Hypotheses
1. Collecting relevant information.
2. Making additional observations.
3. Devise an experiment.
Supports or disproves hypothesis.
Many variables (contributing factors) may
be present.
 The Inductive Method
Described by Francis Bacon
Making numerous observations until one becomes
confident in drawing generalizations and predictions
Knowledge of anatomy obtained by this method

Proof in science
Reliable observations, repeatedly confirmed
Not falsified by any credible observation

In science, all truth is tentative

“Proof beyond a reasonable doubt”

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 The Deductive Method
Most physiological knowledge gained by this method
Investigator formulates a hypothesis—an educated
speculation or possible answer to the question
Good hypotheses are consistent with what is already known
and are testable

Falsifiability—if we claim something is scientifically

true, we must be able to specify what evidence it
would take to prove it wrong

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 Redi’s Experiment

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 Experimental Design
Sample size
Number of subjects in a study
Controls
Control group resembles treatment group but does not
receive treatment
Psychosomatic effects
Effects of subject’s state of mind on her or his physiology
Tested by giving placebo to control group
Experimenter bias
Avoided with double-blind study
Statistical testing
Provides statement of probability that treatment was effective
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 Peer Review
Critical evaluation by other experts in the field
Done prior to funding or publication
Done by using verification and repeatability of results

Ensures honesty, objectivity, and quality in science

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 Facts, Laws, and Theories
Scientific fact
Information that can be independently verified
Law of nature
Generalization about the way matter and energy behave
Results from inductive reasoning and repeated
observations
Written as verbal statement or mathematical formula

Theory
An explanatory statement or set of statements derived from
facts, laws, and confirmed hypotheses
Summarizes what we know
Suggests directions for further study

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 Videos
Scientific Method Amoeba Sisters
Scientific method Khan Academy
Scientific Method Crash Course

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 Living in a Revolution
• Modern biomedical science
– Technological enhancements
• Advances in medical imaging have enhanced our
diagnostic ability and life-support strategies

• Genetic Revolution
• Human genome is finished
• Gene therapy is being used to treat disease

• Early pioneers were important

– Established scientific way of thinking
– Replaced superstition with natural laws
1-18
Evolution, Selection, and Adaptation
• Closest relative: chimpanzee
– Difference of only 1.6% in DNA structure
– Chimpanzees and gorillas differ by 2.3%

• Study of evolutionary relationships

– Help us chose animals for biomedical research (the animal
model)
– Rats and mice used extensively due to issues involved with
using chimpanzees

1-19
 Vestiges of Human Evolution

• Vestigial organs—remnants of organs that

apparently were better developed and more
functional in the ancestors of a species, and
now serve little or no purpose
– Piloerector muscle
– Auricularis muscles

1-20
 The Hierarchy of Complexity
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• Organism is composed of
organ systems Organism

• Organ systems composed of

organs

• Organs composed of tissues

• Tissues composed of cells

Organ Tissue
Organ system

• Cells composed of organelles

Cell

• Organelles composed of
Macromolecule
Organelle

molecules

• Molecules composed of Molecule

Atom

atoms
Figure 1.7 1-21
 Anatomical Variation
• No two humans are exactly alike
– 70% most common structure
– 30% anatomically variant
– Variable number of organs
• Missing muscles, extra vertebrae, renal arteries
– Variation in organ locations (situs solitus,
situs inversus, dextrocardia, situs perversus)

1-22
 Anatomical Variation
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Normal

Pelvic kidney Horseshoe kidney

Figure 1.8
Normal

1-23
Variations in branches of the aorta
 Characteristics of Life

• Organization—living things exhibit a higher

level of organization than the nonliving world
around them
• Cellular composition—living matter is always
compartmentalized into one or more cells
• Metabolism—sum of all internal chemical
change: anabolism, catabolism, and excretion
• Responsiveness and movement—sense and
react to stimuli (responsiveness, irritability, or
excitability)
1-24
 Characteristics of Life

• Homeostasis—maintaining relatively stable

internal conditions
• Development—differentiation and growth
• Reproduction—producing copies of
themselves; pass genes to offspring
• Evolution—mutations: changes in genetic
structure

1-25
 Physiological Variation
• Sex, age, diet, weight, physical activity
• Typical physiological values
– Reference man
• 22 years old, 154 lb, light physical activity
• Consumes 2,800 kcal/day
– Reference woman
• Same as man except 128 lb and 2,000 kcal/day
• Failure to consider variation can lead to
overmedication of elderly or medicating
women on the basis of research done on
men
1-26
• Homeostasis—the body’s ability to detect change,
activate mechanisms that oppose it, and thereby
maintain relatively stable internal conditions
• https://youtu.be/Iz0Q9nTZCw4

1-27
 Homeostasis and Negative Feedback

• Walter Cannon (1871–1945)

– Coined the term homeostasis
– State of the body fluctuates (dynamic equilibrium) within
limited range around a set point
– Negative feedback keeps variable close to the set point

• Loss of homeostatic control causes illness or death

1-28
 Negative Feedback Loop
• Body senses a change and activates mechanisms to reverse it—
dynamic equilibrium
• Because feedback mechanisms alter the original changes that triggered
them (temperature, for example), they are called feedback loops
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1 Room temperature
fallsto66°F(19°C)

C10°
15°20°25°
6 Room cools down
F50°
60°70°80°

2 Thermost atactivates
furnace
C10°
15°20°25°

F50°
60°70°80°

5 Thermostat shuts Figure 1.9a

off furnace

4 Room temperature
rises to 70°F (21°C)

3 Heat output
1-29
(a)
 Negative Feedback
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75
Furnace turned
off at 70 oF
Room temperature (oF)

70

Set point 68 oF

65

Furnace turned
on at 66 oF
60
Time
Figure 1.9b
(b)

• Example: Room temperature does not stay at set point

of 68°F—it only averages 68°F
1-30
 Negative Feedback
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Sweating

Core body temperature

37.5 oC
(99.5 Vasodilation
oF)

37.0 oC Set point

(98.6
o
F)
Vasoconstriction
36.5 oC
(97.7
o
F)
Time Figure 1.10

Shivering

• Example: Brain senses change in blood temperature

– If too warm, vessels dilate (vasodilation) in the skin and
sweating begins (heat-losing mechanism)
– If too cold, vessels in the skin constrict (vasoconstriction)
and shivering begins (heat-gaining mechanism) 1-31
 Homeostatis and Negative Feedback

• Sitting up in bed causes a drop in blood pressure in

the head and upper torso region (local imbalance in
homeostasis); detected by baroreceptors
• Baroreceptors (sensory nerve endings) in the
arteries near the heart alert the cardiac center in
the brainstem. They transmit to the cardiac center

1-32
 Homeostatis and Negative Feedback

• Cardiac center sends nerve signals that increase

the heart rate and return the blood pressure to
normal; regulates heart rate
• Failure of this to feedback loop may produce
dizziness in the elderly

1-33
Postural Change in Blood Pressure
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Person rises
from bed
Blood pressure rises Blood drains from
to normal; homeostasis upper body, creating
is restored homeostatic imbalance

Cardiac center
accelerates heartbeat Baroreceptors above
heart respond to drop
in blood pressure

Figure 1.11

Baroreceptors send signals

to cardiac center of brainstem
Homeostasis and Negative Feedback

• Receptor—senses change in the body (e.g.,

stretch receptors that monitor blood pressure)

• Integrating (control) center—control center

that processes the sensory information,
“makes a decision,” and directs the response
(e.g., cardiac center of the brain)

• Effector—carries out the final corrective

action to restore homeostasis (e.g., cell or
organ)

1-35
Positive Feedback and Rapid Change

• Self-amplifying cycle
– Leads to greater change in the same direction
– Feedback loop is repeated—change produces
more change
• Normal way of producing rapid changes
– Occurs with childbirth, blood clotting, protein
digestion, fever, and generation of nerve signals

1-36
Positive Feedback and Rapid Change
• During birth, the head of the fetus pushes
against the cervix and stimulates its
nerve endings
– Hormone oxytocin is secreted from the pituitary
gland
– Oxytocin travels through the bloodstream to the
uterus stimulating it to contract
– This action pushes the fetus downward toward
cervix, thus stimulating the cervix more, causing
the positive feedback loop to be repeated

1-37
 Positive Feedback Loops
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3 Brain stimulates
pituitary gland to
secrete oxytocin

4
Oxytocin stimulates uterine
2 Nerve impulses contractions and pushes
from cervix fetus toward cervix
transmitted
to brain

1 Head of fetus
pushes against cervix

1-38
Positive Feedback and Rapid Change

• Fever > 104°F

– Metabolic rate increases
– Body produces heat even faster
– Body temperature continues to rise
– Further increasing metabolic rate
• Cycle continues to reinforce itself
• Becomes fatal at 113°F

1-39
 Medical Imaging
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• Radiography (X-rays)
– William Roentgen’s
discovery in 1885
– Penetrate tissues to
darken photographic film
beneath the body
– Dense tissue appears
white
– Over half of all medical
imaging
– Until 1960s, it was the
only method widely
available
(a) X-ray (radiograph)
© U.H.B. Trust/Tony Stone Images/Getty Imagese

Figure 1.13a 1-40

 Medical Imaging
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display.

• Radiopaque substances
– Injected or swallowed
– Fills hollow structures
• Blood vessels
• Intestinal tract

Figure 1.13b
(b Cerebral angiogram
Custom Medical Stock Photos, Inc.

1-41
 Medical Imaging
• Computed tomography
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(CT scan)
– Formerly called a CAT
scan
– Low-intensity X-rays and
computer analysis
• Slice-type image
• Increased sharpness of
image

Figure 1.13c (c) Computed tomographic (CT) scan

© CNR/Phototake

1-42
 Medical Imaging—Nuclear Medicine
• Positron emission tomography
Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display. (PET) scan
– Assesses metabolic state of tissue
– Distinguished tissues most active
at a given moment
– Mechanics—inject radioactively
labeled glucose
• Positrons and electrons collide
• Gamma rays given off
• Detected by sensor
• Analyzed by computer
(d) Positron emission tomographic • Image color shows tissues using
(PET) scan
Tony Stone Images/Getty Images the most glucose at that moment
Figure 1.13d • Damaged tissues appear dark
1-43
 Medical Imaging
• Magnetic resonance Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.

imaging (MRI)
– Slice-type image
– Superior quality to CT scan
– Best for soft tissue
– Mechanics
• Alignment and realignment
of hydrogen atoms with
magnetic field and radio
waves
• Varying levels of energy
given off used by computer
to produce an image (e) Magnetic resonance image (MRI)
© Monte S. Buchsbaum, Mt. Sinai School of Medicine, New York, NY

Figure 1.13e 1-44

 Medical Imaging
• Sonography
– Second oldest and
second most widely
used
– Mechanics
• High-frequency sound
waves echo back
from internal organs
– Avoids harmful X-rays
• Obstetrics
• Image not very sharp
Figure 1.14

1-45
 Chapter 2

The Chemistry of Life

Part 1
 Introduction

Biochemistry
The study of the molecules that compose living
organisms
Carbohydrates, fats, proteins, and nucleic acids
Useful for understanding cellular structures, basic
physiology, nutrition, and health

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 The Chemical Elements 1

Element—simplest form of matter to have unique chemical

properties
Atomic number of an element—number of protons in its
nucleus
Periodic table
Elements arranged by atomic number
Elements represented by one- or two-letter symbols
24 elements have biological role
6 elements = 98.5% of body weight
Oxygen, carbon, hydrogen, nitrogen, calcium, and
phosphorus

Trace elements in minute amounts, but play vital

roles

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 The Chemical Elements 2

Minerals—inorganic elements extracted from soil

by plants and passed up food chain to humans
Ca, P, Cl, Mg, K, Na, and S
Constitute about 4% of body weight
Important for body structure (Ca crystals in teeth,
bones, etc.)
Important for enzymes’ functions
Electrolytes—mineral salts needed for nerve and
muscle function

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 Atomic Structure

Neils Bohr proposed planetary model of atomic structure in 1913

Nucleus—center of atom
Protons: single (+) charge; mass = 1 atomic mass unit (amu)
Neutrons: no charge; mass = 1 amu
Atomic mass is approximately equal to total number of protons
and neutrons

Electrons—in concentric clouds surrounding nucleus

Electrons: single (-) charge, very low mass
An atom is electrically neutral, as number of electrons equals
number of protons

Valence electrons orbit in the outermost shell and determine

chemical bonding properties of an atom

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 Copyright © McGraw-Hill Education. Permission required for reproduction or display.

Figure 2.1

Bohr Planetary Models of Elements

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 Isotopes and Radioactivity 1

Isotopes—varieties of an element that differ only

in the number of neutrons
Extra neutrons increase atomic weight
Isotopes of an element are chemically similar because
they have the same number of valence electrons

Atomic weight (relative atomic mass) of an

element accounts for the fact that an
element is a mixture of isotopes

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 Copyright © McGraw-Hill Education. Permission required for reproduction or display.
Isotopes of
Hydrogen

Figure 2.2

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 Isotopes and Radioactivity 2
Radioisotopes
Unstable isotopes that decay and give off radiation

Intense radiation can cause genetic mutations and cancer

Examples: UV radiation, X-rays, radioactive iodine

Physical half-life of radioisotopes

Time required for 50% to decay to a stable state

Biological half-life of radioisotopes

Time required for 50% to disappear from the body

Cesium 137 has a physical half-life of 30 years, but biological half-life of 17 days

Radioactive iodine has physical half-life of 8 days, but the majority of it is out of the
human body after 2-3 days

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 Radiation and Madame Curie

First woman to receive Copyright © McGraw-Hill Education. Permission required for reproduction or display.

Nobel Prize (1903)

First woman in world to
receive a Ph.D.
Coined term radioactivity
Trained physicians in use of
X-rays and pioneered
radiation therapy as
cancer treatment

Died of radiation
poisoning at age 67

© Science Source

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 Ions, Electrolytes, and Free Radicals 1

• Ion—charged particle (atom or molecule) with

unequal number of protons and electron
• Ionization—transfer of electrons from one atom
to another
• Anion—particle that gains electron(s) (net
negative charge)
• Cation—particle that loses electron(s) (net
positive charge)
• Ions with opposite charges are attracted to
each other

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 Ionization Copyright © McGraw-Hill Education. Permission required for reproduction or display.

1) Transfer of an electron from a sodium atom to a chlorine atom

Figure 2.4

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 Ions, Electrolytes, and Free Radicals 2

Electrolytes—substances that ionize in water and form

solutions capable of conducting electric current

Electrolyte importance
Chemical reactivity, osmosis, electrical excitability of
nerve and muscle
Electrolyte balance is one of the most important
considerations in patient care (imbalances can lead to
coma or cardiac arrest)

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 Ions, Electrolytes, and Free Radicals 3

Free radicals—short-lived particles with an unusual

number of electrons
Produced by normal metabolic reactions, radiation,
certain chemicals
Trigger reactions that destroy molecules, and can cause
cancer, death of heart tissue, and aging

Antioxidants
Chemicals that neutralize free radicals
Superoxide dismutase (SOD) is an antioxidant enzyme in
the body
Selenium, vitamin E, vitamin C, and carotenoids are
antioxidants obtained through the diet

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 Chapter 2

Chemistry Part 2:
Chemical bonds, water and pH
 Molecules and Chemical Bonds 1

Molecule—chemical particle composed of two or more atoms

united by a chemical bond
Compound—molecule composed of two or more different
elements
Molecular formula—identifies constituent elements and how
many atoms of each are present
Structural formula—identifies location of each atom
Isomers—molecules with identical molecular formulae but
different arrangement of their atoms

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 Structural Isomers, Ethanol and Ethyl Ether

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Figure 2.5

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 Molecules and Chemical Bonds 2

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 Molecules and Chemical Bonds 3

Chemical bonds—hold atoms together within a

molecule or attract one molecule to another

Most important types of chemical bonds: ionic

bonds, covalent bonds, hydrogen bonds, van
der Walls forces

Ionic bonds
Attractions between anions and cations (example,
NaCl)

Electrons donated from one atom to another

Easily broken by water

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 Single Covalent Bond

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(a)

Figure 2.6a

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 Double Covalent Bond

Copyright © McGraw-Hill Education. Permission required for reproduction or display.

(b)

Figure 2.6b

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 Molecules and Chemical Bonds 4

Nonpolar bond: electrons shared equally

(strongest bond)
Polar bond: electrons shared unequally (spend
more time near oxygen)

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 Nonpolar and Polar Covalent Bonds

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(a)

(b)
Figure 2.7

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Ionic vs covalent bonding
 Molecules and Chemical Bonds 5

Hydrogen bond—a weak attraction between a

slightly positive hydrogen atom in one molecule
and a slightly negative oxygen or nitrogen atom
in another
Water molecules are attracted to each other by
hydrogen bonds
Large molecules (DNA and proteins) shaped by
hydrogen bonds within them
Important to physiology

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 Hydrogen Bonding of Water

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Figure 2.8

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 Molecules and Chemical Bonds 6

Van der Waals forces—weak, brief attractions

between neutral atoms
Fluctuation in electron density within an atom creates
polarity for a moment, and attracts adjacent atom
for a very short time
Only 1% as strong as a covalent bond, but important
in physiology (example, protein folding)

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 Water and Mixtures

Mixtures—physically blended but not chemically

combined
Body fluids are complex mixtures of chemicals
Most mixtures in our bodies consist of
chemicals dissolved or suspended in water
Water is 50% to 75% of body weight
Depends on age, sex, fat content, etc.

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 Water 1

Polar covalent bonds and a V-shaped molecule

give water a set of properties that account for
its ability to support life.
Solvency
Cohesion
Adhesion
Chemical reactivity
Thermal stability

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 Water 2

Solvency—ability to dissolve other chemicals

Water is called the universal solvent

Hydrophilic—substances that dissolve in water
Molecules must be polarized or charged (e.g., sugar)

Hydrophobic—substances that do not dissolve in water

Molecules are nonpolar or neutral (e.g., fats)

Metabolic reactions depend on solvency of

water

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 Water and Hydration Spheres

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Figure 2.9

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 Water 3

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Ionic solutions
 Water 4

Adhesion—tendency of one substance to cling to

another
Water adheres to large membranes reducing friction
around organs

Cohesion—tendency of like molecules to cling to

each other
Water is very cohesive due to its hydrogen bonds
Surface film on surface of water is due to molecules
being held together by surface tension

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 Water 6

Water’s thermal stability helps stabilize the

internal temperature of the body

Water has high heat capacity—the amount of heat

required to raise the temperature of 1 g of a
substance by 1°C

Calorie (cal)—the amount of heat that raises the

temperature of 1 g of water 1°C
Hydrogen bonds inhibit temperature
increases by inhibiting molecular motion

Effective coolant
1 mL of perspiration removes 500 calories

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 Water 5

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 Solutions, Colloids, and Suspensions 1

Solution—consists of particles called the solute mixed

with a more abundant substance (usually water)
called the solvent
Solute can be gas, solid, or liquid
Solutions are defined by the following properties:
Solute particles under 1 nm
Solute particles do not scatter light
Will pass through most membranes
Will not separate on standing

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 A Solution, a Colloid, and a Suspension

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(a-d): © Ken Saladin

Figure 2.10

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 Solutions, Colloids, and Suspensions 2

Colloids in the body are often mixtures of protein

and water
Many can change from liquid to gel state within and
between cells

Colloids are defined by the following physical

properties:
Particles range from 1–100 nm in size
Scatter light and are usually cloudy
Particles too large to pass through semipermeable
membrane
Particles remain permanently mixed with the solvent
when mixture stands

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 Solutions, Colloids, and Suspensions 3

Suspension
Defined by the following physical properties:
Particles exceed 100 nm
Too large to penetrate selectively permeable
membranes
Cloudy or opaque in appearance
Separates on standing
Example: blood cells are suspended in plasma

Emulsion
Suspension of one liquid in another that are not usually able to
mix
Example: fat in breast milk is an emulsion
Bile salts are great emulsifiers

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 Acids, Bases, and pH 1

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 Acids, Bases, and pH 2

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 The pH Scale

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Figure 2.11

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 Chapter 2

Chemistry: macromolecules
 Energy and Work 1

Energy—capacity to do work
To do work means to move something
All body activities are forms of work

Potential energy—energy stored in an object, but not

currently doing work
Example: water behind a dam
Chemical energy—potential energy in molecular bonds
Free energy—potential energy available in a system to do
useful work

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 Energy and Work 2

Kinetic energy—energy of motion, doing work

Example: water flowing through a dam, generating
electricity
Heat—kinetic energy of molecular motion

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 Classes of Chemical Reactions 1

Chemical reaction—a process in which a covalent

or ionic bond is formed or broken

Chemical equation—symbolizes the course of a

chemical reaction
Reactants (on left)  products (on right)

Classes of chemical reactions

Decomposition reactions
Synthesis reactions
Exchange reactions

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 Classes of Chemical Reactions 2

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 Decomposition Reaction
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(a) Decomposition reaction

Figure 2.12a

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 Synthesis Reaction
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(b) Synthesis reaction

Figure 2.12b

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 Exchange Reaction
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(c) Exchange reaction

Figure 2.12c

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 Classes of Chemical Reactions 3

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 Reaction Rates

Reactions occur when molecules collide with

enough force and correct orientation
Reaction rates increase when…
the reactants are more concentrated
the temperature rises
a catalyst is present
Enzyme catalysts bind to reactants and hold them
in orientations that facilitate the reaction

Catalysts are not changed by the reaction and can

repeat the process frequently

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 Metabolism, Oxidation, and Reduction 1

Metabolism—all chemical reactions of the body

Catabolism
Energy-releasing (exergonic) decomposition reactions
Breaks covalent bonds

Produces smaller molecules

Anabolism
Energy-storing (endergonic) synthesis reactions
Requires energy input
Production of protein or fat

Catabolism and anabolism are inseparably linked

Anabolism is driven by energy released by catabolism

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 Metabolism, Oxidation, and Reduction 2

Oxidation
A chemical reaction in which a molecule gives up
electrons and releases energy
Molecule oxidized in this process
Electron acceptor molecule is the oxidizing agent
Oxygen is often involved as the electron acceptor

Reduction
Any chemical reaction in which a molecule gains
electrons and energy
Molecule is reduced when it accepts electrons
Molecule that donates electrons is the reducing agent

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 Metabolism, Oxidation, and Reduction 3

Oxidation-reduction (redox) reactions

Oxidation of one molecule is always accompanied by
reduction of another
Electrons are often transferred as hydrogen atoms

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 Carbon Compounds
and Functional Groups
1
Organic chemistry—the study of compounds
containing carbon
Four categories of carbon compounds
Carbohydrates
Lipids
Proteins
Nucleic acids

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 Carbon Compounds
and Functional Groups
2
Carbon has four valence electrons
Binds with other atoms that can provide it with four
more electrons to fill its valence shell

Carbon atoms bind readily with each other to form

carbon backbones
Form long chains, branched molecules, and rings
Form covalent bonds with hydrogen, oxygen, nitrogen,
sulfur, and other elements

Carbon backbones carry a variety of functional groups

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Carbon Compounds and Functional Groups 3

Functional groups—small clusters of atoms

attached to carbon backbone

Determine many of the properties of organic

molecules

Examples: hydroxyl, methyl, carboxyl, amino,

phosphate

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 Functional Groups of Organic Molecules

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Name and
Symbol Structure Occurs in

Sugars,
alcohols

Fats, oils,
steroids,
amino acids

Amino acids,
sugars,
proteins

Amino acids,
proteins

Nucleic acids, Figure 2.13

ATP

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 Monomers and Polymers 1

Macromolecules—very large organic molecules

with high molecular weights

Polymers—macromolecules made of a repetitive

series of identical or similar subunits
(monomers)
Starch is a polymer of about 3,000 glucose monomers

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 Monomers and Polymers 2

Dehydration synthesis (condensation) is how living cells

form polymers
A hydroxyl (-OH) group is removed from one monomer,
and a hydrogen (-H) from another
Producing water as a by-product

Hydrolysis—digestion; the opposite of dehydration

synthesis
A water molecule ionizes into –OH and -H
The covalent bond linking one monomer to the other is
broken
The -OH is added to one monomer
The -H is added to the other
Splitting a polymer by the addition of a water molecule

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Dehydration Synthesis and Hydrolysis Reactions

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(a) Dehydration synthesis

(b) Hydrolysis

Figure 2.14

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 Carbohydrates 1

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 The Three Major Monosaccharides

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Figure 2.15

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 Carbohydrates 3

Disaccharide—sugar made of two monosaccharides

Three important disaccharides

Sucrose—table sugar
Glucose + fructose
Lactose—sugar in milk
Glucose + galactose

Maltose—grain products
Glucose + glucose

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 The Three Major Disaccharides

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Figure 2.16

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 Carbohydrates 4

Oligosaccharides—short chains of 3 or more monosaccharides

(at least 10)
Polysaccharides—long chains of monosaccharides (at least 50);
three key examples:
Glycogen—energy storage in cells of liver, muscle, brain, uterus,
vagina
Starch—energy storage in plants that is digestible by humans
Cellulose—structural molecule in plants that is important for human
dietary fiber (but indigestible to us)

Carbohydrates are a quickly mobilized source of energy

All digested carbohydrates converted to glucose
Oxidized to make ATP

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 Glycogen

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Figure 2.17

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 Lipids 1

Lipids are hydrophobic organic molecules with a high

ratio of hydrogen to oxygen
“Afraid of water”

Have more calories per gram than carbohydrates

Five primary types in humans

Fatty acids
Triglycerides
Phospholipids
Eicosanoids
Steroids

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 Lipids 2

Fatty acids
Saturated fatty acids are full of hydrogen, made of
single bonds between carbons
Unsaturated fatty acids contain some double bonds
between carbons in chain (potential to add
hydrogen)
Polyunsaturated fatty acids have multiple
double bonds between carbons in chain

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 Lipids 3
Triglycerides (Neutral Fats)
Three fatty acids linked to glycerol
Each bond formed by dehydration synthesis
Broken down by hydrolysis

Triglycerides at room temperature

When liquid, called oils
Often polyunsaturated fats from plants

When solid, called fat

Saturated fats from animals

Primary function: energy storage

Also help with insulation and shock absorption (adipose tissue)

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 Triglyceride (Fat) Synthesis 1

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Figure 2.18a

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 Triglyceride (Fat) Synthesis 2

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Figure 2.18b

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 Lipids 4

Phospholipids—similar to neutral fats except one

fatty acid is replaced by a phosphate group

Structural foundation
of cell membrane

Amphipathic
Fatty acid “tails” are hydrophobic
Phosphate “head” is hydrophilic

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 Lecithin, a Representative Phospholipid

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Figure 2.20

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 Lipids 5

Eicosanoids
20-carbon compounds derived from arachidonic acid

Hormone-like chemical signals between cells

Includes prostaglandins
Role in inflammation, blood clotting, hormone action, labor contractions,
blood vessel diameter
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 Lipids 6

Steroid—a lipid with 17 carbon atoms in four rings

Cholesterol—the “parent” steroid from which the
other steroids are synthesized
Important for nervous system function and structural
integrity of all cell membranes
15% of our cholesterol comes from diet
85% is internally synthesized (mostly in liver)

Other steroids: cortisol, progesterone,estrogens,

testosterone, and bile acids

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 Cholesterol

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Figure 2.22

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 “Good” and “Bad” Cholesterol

There is only one kind of cholesterol

Does more good than harm

“Good” and “bad” cholesterol refer to droplets of

lipoprotein in the blood
Complexes of cholesterol, fat, phospholipid, and protein

HDL (high-density lipoprotein): “good” cholesterol

Lower ratio of lipid to protein
May help to prevent cardiovascular disease

LDL (low-density lipoprotein): “bad” cholesterol

High ratio of lipid to protein
Contributes to cardiovascular disease

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 Proteins 1

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 Amino Acids

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Some polar amino acids
Some nonpolar amino acids

Methionine Cysteine

Amino acids differ

only in the R
group
Figure 2.23a Tyrosine Arginine

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 Proteins 2

Peptide—any molecule composed of two or more

amino acids joined by peptide bonds

Peptide bond—joins the amino group of one amino

acid to the carboxyl group of the next
Formed by dehydration synthesis

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 Peptide Bond Formation

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Dehydration synthesis creates a peptide bond that joins the

amino acid of one group to the carboxyl group of the next.

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 Protein Structure 1

Conformation— the unique, three-dimensional

shape of protein is crucial to function
Proteins can reversibly change conformation and thus
function
Important examples seen in muscle contraction,
enzyme catalysis, membrane channel opening

Denaturation
Extreme conformational change that destroys function
Extreme heat or pH

Example: when you cook an egg

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 Protein Structure 2

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 Protein Structure 3

Tertiary structure
Further bending and folding of proteins into globular and
fibrous shapes due to hydrophobic-hydrophilic
interactions and van der Waals forces
Globular proteins—compact tertiary structure
for proteins within cell membrane and proteins
that move freely in body fluids
Fibrous proteins—slender filaments suited for
roles in muscle contraction and strengthening
of skin and hair

Quaternary structure
Associations of two or more polypeptide chains due to
ionic bonds and hydrophobic-hydrophilic interactions
Occurs only in some proteins
Example: hemoglobin has four peptide chains

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 Four Levels of Protein Structure Copyright © McGraw-Hill Education. Permission required for reproduction or display.

Primary structure

Sequence of amino acids

joined by peptide bonds

Secondary structure

Alpha helix or beta sheet

formed by hydrogen
bonding

Tertiary structure

Folding and coiling due

to interactions among R
groups and between R
groups and surrounding
water

Quaternary structure

Association of two or
more polypeptide chains
with each other

Figure 2.24

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 Protein Functions 1

Structure
Keratin—tough structural protein of hair, nails, skin surface
Collagen—contained in deeper layers of skin, bones, cartilage, and
teeth
Communication
Some hormones and other cell-to-cell signals are proteins
Ligand—a molecule that reversibly binds to a protein
Receptors to which signal molecules bind are proteins
Membrane transport
Channel proteins in cell membranes govern what passes
Carriers—transport solutes to other side of membrane
Catalysis
Most enzymes are globular proteins

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 Protein Functions 2
Recognition and protection
Glycoproteins are important for immune recognition
Antibodies are proteins

Movement
Motor proteins—molecules with the ability to change shape repeatedly

Cell adhesion
Proteins bind cells together
Example: sperm to egg

Keeps tissues from falling apart

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 Enzymes and Metabolism

Enzymes—proteins that function as biological

catalysts
Permit reactions to occur rapidly at body temperature

Substrate—substance enzyme acts upon

Naming convention
Named for substrate with -ase as the suffix
DNA polymerase

Enzymes lower activation energy—energy needed

to get reaction started

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 Effect of an Enzyme on Activation Energy

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(a) Reaction occurring without a catalyst (b) Reaction occurring with a catalyst

Figure 2.26

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 Enzyme Structure and Action 1

Enzyme action
Substrate approaches enzyme’s active site
Molecules bind together forming enzyme–substrate
complex
Enzyme–substrate specificity—lock and key

Enzyme releases reaction products

Enzyme unchanged and can repeat process

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 Enzyme Structure and Action 3
Reusability of enzymes
Enzymes are not consumed by the reactions

Astonishing speed
One enzyme molecule can consume millions of substrate molecules per
minute
Temperature, pH and other factors can change enzyme shape
and function
Can alter ability of enzyme to bind to substrate
Enzymes vary in optimum pH
Salivary amylase works best at pH 7.0
Pepsin in stomach works best at pH 2.0
Temperature optimum for human enzymes—near body temperature (37°C)
Fever can make reactions happen faster-why?
Extreme fever over 113F can be deadly-why?

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 Cofactors

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 ATP, Other Nucleotides, and
Nucleic Acids

Three components of nucleotides

Nitrogenous base (single or double carbon–nitrogen ring)
Sugar (monosaccharide)
One or more phosphate groups

Adensosine Triphosphate (ATP)—best-known

nucleotide
Adenine (nitrogenous base)
Ribose (sugar)
Phosphate groups (3)

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 ATP and cAMP

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(a) Adenosine triphosphate (ATP) (b) Cyclic adenosine monophosphate (cAMP)

ATP contains adenine, ribose, and three phosphate groups

Figure 2.29

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 Adenosine Triphosphate 1

ATP is body’s most important energy-transfer molecule

Stores energy gained from exergonic reactions
Releases it within seconds for physiological work
Holds energy in covalent bonds
Second and third phosphate groups have high energy
bonds (~)
Most energy transfers to and from ATP involve adding or
removing the third phosphate

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 Source and Uses of ATP

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Figure 2.30

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 Other Nucleotides

Guanosine triphosphate (GTP)

Another nucleotide involved in energy transfer

Cyclic adenosine monophosphate (cAMP)

Formed by removal of second and third phosphate
groups from ATP
Formation triggered by hormone binding to cell surface
cAMP becomes “second messenger” within cell

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 Nucleic Acids
Polymers of nucleotides
DNA (deoxyribonucleic acid)
Contains millions of nucleotides
Constitutes genes
Original blueprint for making the cell’s proteins

RNA (ribonucleic acid)—three types

Messenger RNA (mRNA), ribosomal RNA (rRNA), transfer RNA (tRNA)
Copies of the DNA information that must work together at the ribosome to
make the cell’s proteins

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