The Structure and Functions of Biological Molecules

CHAPTER 2
The Structure and Functions of Biological Molecules
Copyright 2013 John Wiley & Sons, Inc. All rights reserved.
Keys
Define the chemical principles that form the basis of life.

Clarify the principle of chemical bonding (covalent and noncovalent).
Explain ionization.
Describe the chemistry of water and its relationship to cell biology.
Explain the chemistry of hydrophobic and hydrophilic molecules.
Define acids, bases, pH, and buffers.
Describe the structure-function: four groups of macromolecules.
Highlight the similarities and differences between macromolecules.
Explain the importance of polymerization to the production of
macromolecules.
Emphasize the importance of shape in biological chemistry.
2013 John Wiley & Sons, Inc. All rights reserved.
Introduction
Understanding cellular function requires
knowledge of structure.
Structure and function in cells is closely related
to the structure of molecules and atoms.
The study of chemistry is essential for
understanding cell biology.
(2.1) Covalent Bonds

Bonds between atoms with
shared pairs of electrons
are called covalent
bonds.
Molecules are stable
combinations of atoms held
together by covalent bonds.
Compounds are molecules
with more than one type of
atom.
A representation of the
arrangement of electrons in a
number of common atoms
Covalent Bonds
Polar and Nonpolar
Molecules
Polar molecules
have asymmetric
distributions of
electrical charge.
Nonpolar
molecules lack
polarized bonds.
Some biological
molecules, such
as proteins and
phospholipids,
have both polar
and nonpolar
regions.
A representation of the
arrangement of electrons in a
number of common atoms
Covalent Bonds
Atoms tend fill their outer electron shell by sharing electrons with other atoms.
Hydrogen forms a single covalent bond by sharing its unpaired electron.
Oxygen forms two covalent bonds by sharing two unpaired electrons.
Water results when oxygen bonds with two hydrogens.
It requires 80100 kilocalories to break a mole of covalent bonds.
Multiple bonds are formed when more than one pair of electrons are shared by two atoms.
Shared electrons stay closest to the nucleus with the highest electronegativity.
Depends upon the number of protons in nucleus.
Depends upon the distance of the shard electrons from the nucleus.
The Human Perspective:

Free Radicals as a Cause of
Aging
Ionization
Ions result when strongly electronegative nuclei capture
electrons.
Anions have extra electrons.
Cations have lost electrons.
Free radicals are unstable atoms or molecules with
unpaired electrons.
They are formed during normal metabolism.
Are highly reactive and damage macromolecules such as
DNA.
May play a role in aging.

Free Radicals as a Cause of
Aging
Superoxide dismutase (SOD) is an enzyme that destroys
the superoxide radical (O2.).
SOD protects cells from damage due to the superoxide radical.
SOD extends the life span of laboratory animals that overproduce
it.
Calorie restriction:
Extends the lifespan of experimental animals.
Results in decreased production of free radicals.
A new study indicates that individuals on a diet
containing 25% fewer calories show reduced levels of
DNA damage.
(2.2) Noncovalent Bonds

Non-covalent bonds are attractive forces that are weaker
than covalent bonds.
Weak bonds are broken and re-formed.
Weak bonds play an important role in dynamic cellular
processes.
Types of non-covalent bonds
1. Ionic bonds
attractions between
charged atoms.
Are weakened in the
presence of water.
They may be
significant within large
biological molecules.
The dissolution of a salt crystal.

Noncovalent Bonds
Noncovalent ionic bonds between DNA

and protein
Hydrogen bonds
2. Hydrogen bonds:
-- A hydrogen bond occurs when covalently bound hydrogen
has a partial positive charge and attracts electrons of a second
atom.
-- H-bonds determine the structure and properties of water.
-- H-bonds occur in biological molecules, such as between the
strands of DNA. 2013 John Wiley & Sons, Inc. All rights reserved.
Noncovalent Bonds
3. Hydrophobic interaction
and van de Waals forces:
- These occur when nonpolar
molecules associate and
minimize their exposure to
polar molecules.
- van der Waals forces, or
attractions between
nonpolar molecules, are due
to transient dipole formation.
Hydrophobic interactions
reduce exposure to
hydrophilic molecules
Noncovalent Bonds
3. Hydrophobic interaction
and van de Waals forces:
- These occur when nonpolar
molecules associate and
minimize their exposure to
polar molecules.
- van der Waals forces, or
attractions between
nonpolar molecules, are due
to transient dipole formation.
Van der Waals forces operate

at optimum distances and are
maximized by complementary
surfaces.
Noncovalent Bonds
The Life-Supporting Properties of Water

The structure of water is suitable for
sustaining life.
It is asymmetric both H atoms
are on one side.
Both covalent OH bonds are
highly polarized.
All three atoms readily form Hbonds.
Hydrogen bond formation

between neighboring water
molecules
Noncovalent Bonds
The Life-Supporting
Properties of Water
The properties of water
result from its structure.
It is asymmetric
both H atoms are on
one side.
It requires a lot heat
to evaporate it.
It is an excellent
solvent for many
substances.
The importance of water
in protein structure
It determines the
interactions between
many biological
solutes. 2013 John Wiley & Sons, Inc. All rights reserved.
(2.3) Acids, Bases, and Buffers

Acids release protons.
Bases accept protons.
Amphoteric molecules can act as either acids or
bases. For example, water:
H3O H+ + H2O OH + H+
Acid
Amphoteric
Base
molecule
Acidity is measure using the pH scale.

pH = log [H+]
The ion product constant for water is
Kw = [H+][OH] = 10-14 at 25 C.
As [H+] increases, [OH] decreases so that the product
equals 1014.
Acids, Bases, and Buffers

Biological processes are sensitive to pH.
Changes in pH affect the ion state and function of
proteins.
Buffers in living systems resist changes in pH.
For example, bicarbonate ions and carbonic acid
buffer the blood: HCO3 + H+ H2CO3
Bicarbonate
ion
Hydrogen
ion
Carbonic
acid
(2.4) The Nature of Biological

Molecules
Carbon is central to the chemistry of life.
Carbon forms four covalent bonds, with itself or other
atoms.
Carbon-containing molecules produced by living organisms
are called biochemicals.
Hydrocarbons:
Contain only carbon
and hydrogen.
Vary in the number
of carbons, and the
number of double
and triple bonds
between carbons.
The Nature of Biological Molecules

Functional groupsgroups of atoms giving organic
molecules different characteristics and properties.
Functional classification of biological molecules:
Macromolecules: large structural and functional molecules in
cells. Include four major categories: proteins, nucleic acids,
polysaccharides and lipids.
The Nature of Biological Molecules

Building blocks of macromolecules
include amino acids, nucleotides,
sugars, and fatty acids.
Metabolic intermediates: compounds
formed in metabolic pathways.
Molecules of miscellaneous function:
include vitamins, hormones, ATP, and
metabolic waste products.
Monomers and polymers:

polymerization and
hydrolysis.
(2.5) Four Types of Biological

Molecules
Carbohydrates include
simple sugars and sugar
polymers.
Lipids are a diverse
group of nonpolar
molecules.
Fats are made of
glycerol linked by three
ester bonds to three
fatty acids.
Proteins are polymers

of amino acids and form
a diverse group of
An overview of the types
macromolecules.
of biological molecules
Nucleic acids are
that make up various
polymers of nucleotides
cellular structures.
that store and transmit
genetic
2013 John Wiley & Sons, Inc. All rights
reserved. information.
Four Types of Biological Molecules

Carbohydrates include simple sugars and sugar polymers.
They serve as energy storage molecules.
Structure:
Chemical formula is (CH2O)n
Ketose sugars have a carbonyl (C=O) on an internal carbon
Aldose sugars have a carbonyl on a terminal carbon.
Sugars can be linear but sometimes form ring structures.
The
structures of
sugars

Carbohydrates
Stereoisomerism:
Asymmetric carbons
bond to four different
groups.
Molecules with
asymmetric carbons can
exist in two mirrorimage configurations
called enantiomers or
stereoisomers.
Enantiomers can be as
either D- or L-isomers.
Sugars can have many
asymmetric carbons,
but are designated D- or
L- according to the
arrangement around the
carbon farthest from the
carbonyl group.
Stereoisomerism of
glyceraldehyde.

Carbohydrates
Stereoisomerism:
Asymmetric carbons
bond to four different
groups.
Molecules with
Aldotetroses
asymmetric carbons
.
can exist in two
mirror-image
configurations called
enantiomers or
stereoisomers.
Enantiomers can be
as either D- or Lisomers.
Sugars can have
many asymmetric
Formation of an - and carbons, but are
pyranose
designated D- or Laccording to the
arrangementaround

Carbohydrates
Linking Sugars Together:
Glycosidic bonds are C
OC links between
sugars.
Disaccharides are used as
a source of readily
available energy.
Oligosaccharides are
found bound to cells
surface proteins and lipids,
and may be used for cell
recognition.
Disaccharides: Sucrose and

lactose
Polysaccharides: identical sugar monomers but dramatically

different properties
Carbohydrates
Polysaccharides are polymers of sugars joined by glycosidic bonds.
Glycogen is an animal product made of branched glucose
polymers.
Starch is a plant product made of both branched and
unbranched glucose polymers.
Polysaccharides: identical sugar monomers but dramatically

different properties
Cellulose, chitin, and glycosaminoglycans (GAGs):

structural polysaccharides
Cellulose: plant product made of unbranched polymers
Chitin: component of invertebrate exoskeleton made
GAGs: composed of two different sugars and found in
extracellular space.
Fats and fatty acids
Lipids are a diverse group of nonpolar molecules.

Fats are made of glycerol linked by three ester bonds to
three fatty acids (Fas).
FAs are unbranched hydrocarbons with one carboxyl group;
they are amphipathic.
Saturated FAs lack C=C double bonds and are solid at room
temperature.
Unsaturated FAs have one or more C=C double bonds and are
liquid at room temperature.

Soaps
consist of
fatty acids
Lipids are a diverse group of nonpolar molecules.

Fats are made of glycerol linked by three ester bonds to
three fatty acids (Fas).
FAs are unbranched hydrocarbons with one carboxyl group;
they are amphipathic.
Saturated FAs lack C=C double bonds and are solid at
room temperature.
Unsaturated FAs have one or more C=C double bonds and
are liquidat
room temperature.
Steroids are four-ringed animal lipids that have been

implicated in atherosclerosis.
Phospholipids are amphipathic lipids that are a major
component of cell membranes.
The phospholipid phosphatidylcholine.

The structure of steroids.
Biological structures composed

predominantly of protein: feathers and the
lenses of eyes
Proteins are polymers of amino acids and

form a diverse group of macromolecules.
They exhibit a high degree of specificity.
They have a variety of cellular functions.

Amino acid
structure. Balland-stick model,
chemical formula,
and peptide bond
formation.
Amino acid stereoisomerism.
The Building Blocks of Proteins

Amino acids have an carbon, an amine group, a carboxyl
group, and a variable R group.
Amino acids in nature occurs as the L stereoisomer.
Amino acids are linked together by peptide bonds into a
polypeptide chain to make a protein.

Amino acid
structure. Balland-stick model,
chemical formula,
and peptide bond
formation.
Amino acid stereoisomerism.
Peptide bonds form between the -carbonyl and the amino of participating amino acids.
Amino acids differ in the R group attached to one of
the bonds of the -carbon.
R groups may be polar charged; polar uncharged;
nonpolar.

The chemical
structures of
amino acids
A. Polar charged - contain R groups that act as stronger

organic acids, bases; can form ionic bonds
1. Almost always fully charged (lysine, arginine,
aspartic acid, glutamic acid) at pH 7; side chains are
relatively strong organic acids & bases
2. Can form ionic bonds due to charges; histones
with arginine (+-charge) bind to negatively charged
phosphate groups of DNA
3. Histidine - usually only partially charged at pH 7;
often
important
in enzyme
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John Wiley & Sons,
Inc. All rights active
reserved. sites due to its

The chemical
structures of
amino acids
B. Polar uncharged - R groups weakly acidic or basic; not fully

charged at pH 7; can form H bonds with other
molecules like water since they have atoms
with a partial negative or positive charge
Asparagine & glutamine [amides of aspartic & glutamic
acid], threonine, serine, tyrosine

The chemical
structures of
amino acids
C. Nonpolar - R groups hydrophobic; generally lack O & N;

cannot interact with water or form electrostatic
bonds; vary primarily in size & shape; allows them
to pack tightly into protein core
1. Alanine, valine, leucine, isoleucine, tryptophan,
phenylalanine, methionine
2. Associate with one another via hydrophobic & van der Waals
interactions in protein core

The chemical
structures of
amino acids
D. The other three glycine, proline, cysteine

1. Glycine (R = H) - small R group makes backbone flexible & able
to move so it is useful in protein hinges; small R group allows 2
backbones (of same or different protein) to approach closely
2. Proline R group forms ring with amino group (imino acid);
hydrophobic amino acid that does not readily fit into orderly secondary
structure (-helix)
3. Cysteine R group has reactive SH; forms disulfide (SS)
bridge with other
cysteines often at some distance away
in polypeptide backbone

R groups may have other properties.
Glycine has only H as its R group
and is small.
The -carbon of proline is part of a
ring, creating kinks in the protein.
Cysteine forms disulfide bridges
(SS) with other cysteines.
The nature of the R groups
determines the function of the
protein.
Post-translational
modifications
Phosphorylation of Tyr, Thr, Ser
Acetylation of Lys
Formation of disulfide
bonds: oxidation and
reduction of bonds between
two cysteine residues
Hydrophobic and hydrophilic

amino acid residues in the protein
cytochrome c
The ionization of
charged, polar amino
acids.
Scanning electron
micrograph:
The -helix: structure and physical characte
Red blood cell sickle cell
anemia of Proteins
The Structure
Primary structure, the sequence of amino acids in the polymer, is
critical to the protein function.
Secondary structure refers to the conformation of adjacent
amino acids into -helix, -sheet, hinges, turns, turns, loops, or
finger-like extensions.
The -pleated sheet: structure and physical characteristics
The Structure of Proteins

Primary structure, the sequence of amino acids in the polymer, is
critical to the protein function.
Secondary structure refers to the conformation of adjacent
amino acids into -helix, -sheet, hinges, turns, turns, loops, or
finger-like extensions.
Types of non-covalent
An X-ray diffraction
bonds maintaining the
Ribbon model
pattern of
conformation of
of
myoglobin
proteins
ribonuclease
Tertiary structure is the conformation of the entire
polymer.
It is stabilized by noncovalent bonds.
It is studied by X-ray crystallography.
Proteins can be fibrous or globular.
The three-dimensional structure of

myoglobin.
Myoglobin: The First Globular Proteins Whose Tertiary

Structure Was Determined
Stores oxygen in muscle cells.
Has a heme prosthetic group that binds O2.
Structure derived using X-ray crystallography.

Proteins
are made
up of
domains
that can
be
conserved
.
Protein Domains
Dynamic movements
within the enzyme
acetylcholinesterase.
Domains occur when proteins are composed of two or more distinct regions.
Each domain is a functional region
Dynamic Changes within Proteins

May occur with protein activity.
Conformational changes are non-random movements
triggered by the binding of a specific molecule.
Hemoglobin: and globin
Quaternary structure refers to proteins

composed of subunits.
Dimer: TGF-2
Cysteine residues
Hydrophobic residues
It refers to the manner in which subunits interact.
Protein-Protein Interactions
Different proteins can become
physically associated to form a
multiprotein complex.
Pyruvate dehydrogenase:
60 polypeptide chains
Proteinprotein
interactions: complementary
molecular surfaces of portions
of two interacting proteins
Can be studied using the yeast two-hybrid (Y2H).
Results from large-scale studies can be presented in the form of a network.
A list of potential interactions can be used to elucidate unknown processes.
A network of proteinprotein
interactions.
Proteinprotein
interactions of hub
proteins.
Can be studied using the yeast two-hybrid (Y2H).

Results from large-scale studies can be presented in the form of a network.
A list of potential interactions can be used to elucidate unknown processes.
Hub proteins most likely more important that non-hub proteins.
Ribonuclease A
(RNase: 124 aa; 4 disulfide
bonds)
Protein Folding is a process

that occurs in various
steps.
Anfinsen observed that

unfolding is due to
denaturation, brought
about by various agents.
Removal of denaturing
Denature:
agents could lead to
- 8M urea (unfold)
refolding.
- -mercaptoethanol: converts SS to
sulfhydryl (SH) groups
- Reversibility of events
- Information of the final 3D
conformation contained within
the
primary sequence

Two alternate pathways for protein
folding:
First step:
Formation of
secondary
structure or
collapse
driven by
hydrophobic
interactions
Proteins may assume their native

conformation through a series of steps.
Proteins may fold along pathways
without intermediate forms.
Smaller proteins with single domains
fold faster than larger proteins with
multiple domains.
Along
the
folding
pathway

Protein Misfolding Can Have Deadly
Consequences
A contrast in
structure between
normal and
infectious prion
protein
Creutzfeld-Jakob Disease (CJD) results from

misfolded protein in the brain.
Healthy brains contain a normal protein, PrP c.
CJD brains have PrPSc, which is identical or similar to PrP c
but is misfolded.
Mad cow disease, kuru, and scrapie are also caused by
PrPSc.

Consequences
Alzheimers disease (AD) involves misfolded proteins that

accumulate in the brains of affected individuals.
A membrane-bound protein in brain neurons, called amyloid
precursor protein (APP), is cleaved by two secretase enzymes.
In individuals genetically predisposed to AD one of the
cleavage products is A42, a protein that misfolds and selfassociates into amyloid plaques.

Consequences
All drugs for treatment of AD are aimed at
management of symptoms.
Pursuit of new drugs for AD aimed at:
Prevent formation of A42 peptide.
Remove the A42 peptide once it has
formed.
Prevent interaction between A
molecules.
Formation of the A
peptide

Consequences
All drugs for treatment of AD are aimed at
management of symptoms.
Pursuit of new drugs for AD aimed at:
Prevent formation of A42 peptide.
Remove the A42 peptide once it has
formed.
Prevent interaction between A
molecules.
Amyloid plaque detection in

normal (top) and diseased
(bottom) brains.

The Role of Molecular Chaperones
Molecular chaperones are helper proteins to prevent
nonselective interactions during protein folding to achieve
proper 3D conformation.
Hsp 70 family bind emerging proteins and prevent
inappropriate interactions.
Chaperonins allow large new proteins to assemble without
interference from other macromolecules. TriC processes up
to 15% of the cells proteins.
The role of molecular

chaperones in encouraging
protein folding
The Emerging Field of Proteomics

The proteome is the entire inventory of an organisms proteins.
Proteomics uses advanced technologies to perform large-scale
studies on diverse proteins.
Proteins are separated using gel electrophoresis.
Proteins are identified using mass spectrometry and high
speed computers.

The proteome is the entire inventory of an organisms proteins.
Proteomics uses advanced technologies to perform large-scale
studies on diverse proteins.
Proteins are separated using gel electrophoresis.
Proteins are identified using mass spectrometry and high
speed computers.
The study of proteomics often requires the separation of complex

mixtures of proteins
Identifying proteins by
mass spectrometry

Protein microarrays (protein chips) allow researchers to screen
proteins for various activities and disorders.
In a near future biotechnology companies will be manufacturing
microarrays containing antibodies for different blood proteins, which
may indicate that a person may be suffering from a particular disease.
Global analysis
of protein
activities using
protein chips.
Protein Engineering
Current technology allows the making of artificial genes that
code for proteins of specific amino acids sequences.
Knowledge of a proteins amino acid sequence rarely allows
prediction of a proteins structure.
Site-directed mutagenesis allows researchers to make
alterations in single amino acids by altering the DNA
encoding a protein.

Structure-Based Drug
Design
Computer simulations
of protein binding sites
are used to design
drugs that inhibit
specific proteins.
An example of such
application is the drug
Gleevec for treatment
of rare cancers.
Computationally
designed proteins that
target viral proteins.
Computational
design of a
protein that is
capable of
binding to the
surface of
another protein.
Development of a proteintargeting drug
Gleevac
structure
ABL protein-targeting
with Gleevac (L) and
Sprycel (R)

Protein Adaptation and Evolution
Adaptations are traits that improve
the chance of survival of an organism
in a specific environment.
Proteins are subject to natural
selection.
Members of a protein family are
thought to have evolved from a
single ancestor gene.
A particular protein may have
different versions (isoforms) that
are tissue- or stage-specific.
Distribution of polar,
charged amino acid
residues in the enzyme
malate dehydrogenase

Protein Adaptation and Evolution
Adaptations are traits that improve
the chance of survival of an organism
in a specific environment.
Proteins are subject to natural
selection.
Members of a protein family are
thought to have evolved from a
single ancestor gene.
A particular protein may have
different versions (isoforms) that
are tissue- or stage-specific.
Protein structure alteration

from a single amino acid
change.

Nucleic acids are polymers of
nucleotides that store and
transmit genetic information.
Deoxyribonucleic acid
(DNA) holds the genetic
information in all cellular
organisms and some viruses.
Ribonucleic acid (RNA) is
the genetic material in some
viruses.
Nucleotides are connected by
3-5 phosphodiester bonds
between the phosphate of
one nucleotide and the 3
carbon of the next.
Nucleotides and
nucleotide
strands of RNA

Each nucleotide consists of
three parts:
A five-carbon sugar
A phosphate group
A nitrogenous base
Bases are either
purines or
pyrimidines.
The purines are
adenine and guanine
in both DNA and RNA.
The pyrimidines are
cytosine and uracil in
RNA; uracil is replaced
by thymine in DNA.
Nitrogenous bases
in nucleic acids
RNA and the ribosome

RNA is usually single stranded and DNA is usually double stranded.
RNA may fold back on itself to form complex three dimensional
structures, as in ribosomes.
RNA may have catalytic activity; such RNA enzymes are called
ribozymes.
Adenosine triphosphate (ATP) is a nucleotide that plays a key role in
cellular metabolism, whereas guanosine triphosphate (GTP) serves
as a switch to turn on some proteins.
(2.6) The Formation of Complex

Molecular Structure
Different types of subunits can self-assemble to form
complex structures.
One example is the tobacco mosaic virus (TMV), which
was shown to self-assemble from ribosomal subunits and
proteins.
Cells may use molecular chaperones to assemble
molecular structures.
Experimental Pathways:
Helping Proteins Reach Their Proper
Folded State
Some proteins can self-assemble from purified
subunits.
Other proteins require molecular chaperones for
proper folding.
Molecular chaperones may protect protein structure
during the heat shock response.
The heat shock response involves synthesis of heat shock
proteins that prevent denaturation of existing proteins.
Folded State
Heat shock proteins and other chaperones prevent
aggregation of denatured or newly synthesized
proteins.
Chaperones also move newly synthesized proteins
across membranes.
The protein GroEL is synthesized in E. coli is essential
for the proper folding of other cellular proteins.
GroEL
models
Folded State
Conformatio
nal change
in GroEL
GroEl acts in conjunction with another

protein, GroES.
Attachment of GroES to GroEL induces a
conformational change in the GroEL
protein.
The GroEL-GroES complex assists a
protein and achieving its native state.
Folded State
GroEL-GroESassisted
folding of a
polypeptide
GroEl acts in conjunction with another protein, GroES.

Attachment of GroES to GroEL induces a
conformational change in the GroEL protein.
The GroEL-GroES complex assists a protein and
achieving its native state.
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CHAPTER 2

The Structure and Functions of Biological Molecules

Define the chemical principles that form the basis of life.

2013 John Wiley & Sons, Inc. All rights reserved.

2013 John Wiley & Sons, Inc. All rights reserved.

(2.1) Covalent Bonds

2013 John Wiley & Sons, Inc. All rights reserved.

2013 John Wiley & Sons, Inc. All rights reserved.

The Human Perspective:

2013 John Wiley & Sons, Inc. All rights reserved.

The Human Perspective:

(2.2) Noncovalent Bonds

The dissolution of a salt crystal.

Noncovalent ionic bonds between DNA

2013 John Wiley & Sons, Inc. All rights reserved.

Van der Waals forces operate

The Life-Supporting Properties of Water

Hydrogen bond formation

(2.3) Acids, Bases, and Buffers

Acidity is measure using the pH scale.

Acids, Bases, and Buffers

2013 John Wiley & Sons, Inc. All rights reserved.

(2.4) The Nature of Biological

The Nature of Biological Molecules

2013 John Wiley & Sons, Inc. All rights reserved.

The Nature of Biological Molecules

Monomers and polymers:

2013 John Wiley & Sons, Inc. All rights reserved.

(2.5) Four Types of Biological

Proteins are polymers

Four Types of Biological Molecules

2013 John Wiley & Sons, Inc. All rights reserved.

Four Types of Biological Molecules

2013 John Wiley & Sons, Inc. All rights reserved.

Four Types of Biological Molecules

Four Types of Biological Molecules

Disaccharides: Sucrose and

2013 John Wiley & Sons, Inc. All rights reserved.

Four Types of Biological Molecules

Polysaccharides: identical sugar monomers but dramatically

Four Types of Biological Molecules

Polysaccharides: identical sugar monomers but dramatically

Cellulose, chitin, and glycosaminoglycans (GAGs):

Four Types of Biological Molecules

Fats and fatty acids

Lipids are a diverse group of nonpolar molecules.

Four Types of Biological Molecules

Lipids are a diverse group of nonpolar molecules.

Four Types of Biological Molecules

Steroids are four-ringed animal lipids that have been

The phospholipid phosphatidylcholine.

Four Types of Biological Molecules

Biological structures composed

Proteins are polymers of amino acids and

Four Types of Biological Molecules

Amino acid stereoisomerism.

The Building Blocks of Proteins

Four Types of Biological Molecules

Amino acid stereoisomerism.

Four Types of Biological Molecules

A. Polar charged - contain R groups that act as stronger

Four Types of Biological Molecules

B. Polar uncharged - R groups weakly acidic or basic; not fully