POWERPOINT LECTURE SLIDE PRESENTATION

by ZARA OAKES, MS, The University of Texas at Austin

Additional text by Jessica Padilla exclusively for Physiology at ECC
UNIT 1

2 Molecular Interactions

HUMAN PHYSIOLOGY
AN INTEGRATED APPROACH FOURTH EDITION

DEE UNGLAUB SILVERTHORN

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About this Chapter
Atoms, ions, and molecules (self review)
Types of chemical bonds (self review)
Biomolecules
Solutions, concentrations, and pH
Water Properties
Protein interactions

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Types of Biomolecules
All four types are composed of either monomers or
covalently linked polymers. The first three provide
energy to the body.
Monomers are connected by dehydration reactions to
create polymers
Polymers are broken down into monomers by
hydrolysis reactions
The four groups of biomolecules (organic
macromolecules) are:
Carbohydrates
Lipids
Proteins
Nucleotides and nucleic acids
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 Most macromolecules are polymers

Polymers are made by stringing together many smaller

molecules called monomers
Cells link monomers by a process called dehydration
synthesis
In this process water is removed to unite the two units
and form a polymer.

Short polymer Monomer

Longer polymer
Figure 3.7A
(a) Dehydration synthesis of a polymer
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 Polymers broken to monomers

Organisms also have to break down macromolecules

Cells do this by a process called hydrolysis
In hydrolysis a water molecule is used to split a bond
between two monomers to reduce the size of the polymer.

Figure 3.7B
(b) Hydrolysis of a polymer
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Carbohydrates
Most abundant
Carbon
Hydrogen
Oxygen
Simple
Monosaccharides (glucose, ribose)
Complex
Polysaccharides (glycogen, starch)
Monomer linked to form polymers by a glycosilic
bond

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Carbohydrates

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Carbohydrates

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Fun Facts

Americans consume an
average of 140 pounds of
sugar per person per year

Cellulose, found in
plant cell walls, is the
most abundant organic
compound on Earth

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Lipids
Carbon and hydrogen (little oxygen)
Structurally diverse
Eicosanoids
Steroids
Phospholipids
Triglycerides
Glycerol
Fatty acid chains
Saturated
Unsaturated
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 High Energy Fuel Source
Larger hydrocarbons

Are the main

molecules in the
gasoline we burn
in our cars

The hydrocarbons
of fat molecules
provide energy for
our bodies

Figure 3.4

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Lipids and Lipid-Related Molecules

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Proteins
Amino acids
Essential
Amino group
Acid group
Protein structure
Polypeptides
Primary through quaternary
Most versatile

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 The four types of proteins

(b) Storage (d) Transport

proteins proteins

(a) Structural proteins

(c) Contractile proteins

Figure 3.18

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Levels of Organization in Protein Molecules

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 Protein Shape
Proteins have four levels of structure

Hydrogen bond

Pleated sheet
Polypeptide
Amino acid (single subunit)

(a) Primary structure

Complete
Hydrogen bond protein,
with four
polypeptide
Alpha helix subunits
(b) Secondary (c) Tertiary
structure structure

(d) Quaternary structure

Figure 3.23
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 Proteins
Various types of bonds interact to create different types of
proteins. The types of bonds that shape the protein affect
the structure.
Fibrous
Globular

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 Nucleic Acids
Composition
Base, sugar, and phosphate(s)
Transmit and store
Information (genetic code)
Energy transfer molecules
ATP, cAMP,
NAD, and FAD

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Nucleotides, DNA, and RNA

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Aqueous Solutions
Aqueous
Water-based
Solution
Solute dissolves in solvent
Solubility
Ease of dissolving
Hydrophobic
Hydrophilic

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Aqueous Solubility
Sodium chloride dissolves in water

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Water properties
Molecular structure
Hydrogen bond-the high amount of hydrogen bond in
water give it properties no found in other substances.
It makes it less dense as a solid and give a high
specific heat.
Surface tension- results from cohesion and adhesion
Cohesion- water molecules stick together
Adhesion-water molecules stick to surfaces
Biological Process
Water can absorb and store large amounts of heat while only
changing a few degrees in temperature thus allowing it to
regulate heat in the body.
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 Water properties
These
illustrate the
properties of
water that
result from
hydrogen
bonding.

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Hydrogen Ion Concentration (pH)-self review
Acid
Contributes H+ to solution
Base
Decreases H+ in solution
pH
- log [H+]
Buffer minimizes changes of pH

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 Hydrogen Ion Concentration (pH)
pH scale

Mechanisms
in the body
closely
regulate blood
ph to protect
from the
harmful
effects of
going beyond
the range.

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Protein Interactions
Human Proteomics Initiative- determine all the
types of proteins in the body.
Protein Solubility- the degree to how water
soluble a protein is determines influences is role in
the body
Insoluble create supportive structures like collagen
and keratin
Soluble- carry out chemical reactions and interact
with molecules
Seven categories- these include enzymes,
membrane transporters, signal molecules, receptors,
binding and regulatory proteins, and antibodies.
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Protein Interactions
Binding- when proteins binds a conformation change called induce fit
occurs. The bind success depends on:
Selectivity- protiens bind specific molecules
Ligand- generic name for molecules that bind and interact
Substrate- ligands that bind enzymes and membrane transporter
Binding site- area where ligand attaches and forms reversible
or irreversible bonds
Specificity- the ability of a protein to bind a certainligand
Affinity- degree to which a protein is attracted to a ligand.
A high disassociation constant indicates low affinity.

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Selective Binding: Induced-Fit Model
The induced-fit model of protein-ligand binding

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 Factors that affect protein binding
Isoforms- proteins with similar function but different affinities for the same
ligand. Ex- fetal vs adult hemoglobin
Activation some inactive proteins undergo a physical alteration to become
active- like protein hormones and enzymes
Cofactors must bind to protein to enhance affinity to ligand, usually its a
functional group or ion.
Lysis cleaving a protein section to activate it.
Modulators influences binding or activity of a protein
Chemical modulators bind covalently or non-covalently to alter binding
or activity by decreasing or increasing it.
Antagonists decreases activity by blocking binding site
Competitive inhibitors reversible antagonists that competitively bind and
can be displaced
Allosteric modulators -reversible antagonists that competitively bind but
can not be displaced
Covalent modulators - bind and alter properties to activate or inactivate-
ex. penicillin
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Modulators Alter Binding or Activity

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Factors that Affect Affinity

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Competitive Inhibition

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Allosteric Modulation

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Allosteric Modulation

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Physical Regulators
Temperature- each protein has a adequate temperature for its
function. Outside of the range it may be denatured of inactivated.

pH- each protein has a adequate temperature for its function. Outside of
the range it may be denatured of inactivated.

Concentration of protein amounts in body vary over time to

control physiological processes
Up-regulation programmed production of protein
Down regulation programmed removal of protein
Concentration of ligand determines the magnitude of the
reponse if the protein concentration is the same.
Reaction rates speed up as ligand concentration increases up
until saturation is reached.

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Summary
Atoms in review
Four types of chemical bonds
Four kinds of biomolecules
Aqueous solutions and pH
Proteins in focus

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