Chapter 2 The Structure and Functions of Biological Molecules, Biols300

CHAPTER 2
The Structure and Functions of

Biological Molecules
© 2013 John Wiley & Sons, Inc. All rights reserved.

1
Keys
• Define the chemical principles that form the basis of

life.
• 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.

2
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.

3
(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.

4
The Nature of Biological Molecules
• Functional groups—groups of atoms giving organic molecules

different characteristics and properties.
• Classification of biological molecules by functions:
1- Macromolecules: large structural and functional molecules in cells.
Include four major categories: proteins, nucleic acids, polysaccharides
and lipids.

5
The Nature of Biological Molecules
2. Building blocks of
macromolecules
(precursors) include amino
acids, nucleotides, sugars,
and fatty acids.
3. Metabolic intermediates
(metabolites): compounds
formed in metabolic
pathways.
4. Molecules of
miscellaneous function:
include vitamins, Monomers and polymers:
hormones, ATP, and polymerization and hydrolysis.
metabolic waste products.

6
(2.5) Four Types of Biological Molecules
1. Carbohydrates include simple

sugars and sugar polymers.
2. Lipids are a diverse group of
nonpolar molecules.
– Fats are made of glycerol
linked by three ester bonds to
three fatty acids.
3. Proteins are polymers of
amino acids and form a
diverse group of
macromolecules.
4. Nucleic acids are polymers of
nucleotides that store and
An overview of the types of
biological molecules that make
transmit genetic information.
up various cellular structures. – Deoxyribonucleic acid (DNA)
and Ribonucleic acid (RNA)

7
Carbohydrates

up various cellular structures.

8
Carbohydrates
Functions
• Sources of energy
• Intermediates in the biosynthesis of other basic
biochemical entities (fats and proteins).
• Associated with other entities such as glycosides,
vitamins and antibiotics.
• Form structural tissues in plants and in
microorganisms (cellulose, lignin).
• Participate in biological transport, cell-cell
recognition, activation of growth factors,
modulation of the immune system.
9
Four Types of Biological Molecules
• Carbohydrates include simple sugars and sugar polymers.
– They serve as structural and 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 (C=O) on a terminal carbon.
• Sugars can be linear but sometimes form ring structures.
The structures
of sugars

10
Structural representation of sugars
Simple sugars can exist in open and closed forms.
• Fisher projection: straight chain representation
• Haworth projection: simple ring in perspective
• Conformational representation: chair and boat configurations
11
Prepared by: Dr. A. Ameer Allaith
• Carbohydrates
– Stereoisomerism:
• Asymmetric carbons
bond to four different
groups.
• Molecules with
asymmetric carbons
can exist in two mirror-
image configurations
called enantiomers or
stereoisomers.
• Enantiomers can be as
either D- or L-isomers.
Stereoisomerism of glyceraldehyde.

12
• Carbohydrates
• Enantiomers can be as
either D- or L-isomers.
• Sugars can have many
asymmetric carbons, Aldotetroses.
but are designated D-
or L- according to the
arrangement around
the carbon farthest
from the carbonyl
group.

13
• Carbohydrates
• Formation of an a- and b-pyranose. When a molecule of glucose undergoes
self-reaction to form a pyranose ring (i.e., a six-membered ring), two
stereoisomers are generated. The two isomers are in equilibrium with each
other through the open-chain form of the molecule. By convention, the
molecule is an alpha-pyranose when the OH group of the first carbon projects
below the plane of the ring, and a beta-pyranose when the hydroxyl group
projects upward.
Formation of an a- and b-pyranose

© 2013 John Wiley & Sons, Inc. All rights reserved. 14
Carbohydrates Classification:
Based on number of monomers
Carbohydrates
Monosaccharaides Disaccharides Oligosaccharides Polysaccharides
Glucose Sucrose Raffinose Glycogen
Fructose Lactose Stachyose Starch
Galactose Maltose Chitin

15
• Carbohydrates
– Linking Sugars Together:
• Glycosidic bonds are –
C—O—C– 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

16
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.

17
Disaccharides
• Disaccharides are used as a

source of readily available
energy.
1. Sucrose (table sugar) - major
component of plant sap; carries
chemical energy from one part of
plant to another.
2. Lactose (milk sugar) - fuel for early
growth & development of
newborns.
a. Enzyme lactase that hydrolyzes
it is found in membranes of cells
lining intestines
b. If lose this enzyme after Disaccharides: Sucrose and lactose
childhood, eating dairy products
causes digestive discomfort
18
Oligosaccharides
Oligosaccharides
Small chains of sugars (oligo - few), usually attached to lipids & proteins converting
them to glycolipids & glycoproteins, respectively
1. Particularly important on plasma membrane from which they project
2. They may be composed of many different combinations of sugar units & can thus
play an informational role
3. They can distinguish one cell type from another & help mediate specific
interactions of a cell with its surroundings

19
20
• 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.

21
• Cellulose, chitin, and glycosaminoglycans (GAGs): structural

polysaccharides
– Cellulose: plant product made of unbranched polymers
– Chitin: component of invertebrate exoskeleton made
– Glycosaminoglycans (GAGs): composed of two different sugars and
found in extracellular space.
22
Polysaccharides
• Glycogen is an animal product

made of branched glucose
polymers mostly joined by α(1—
>4) bonds.
1. Branches every 10 or so units; sugar at branch joined to 3 neighboring units

instead of 2; branch bond is α(1—>6) glycosidic linkage
2. Surplus chemical energy storehouse in most animals; typical MW from 1 - 4
million daltons.
3. Human skeletal muscles have enough glycogen to fuel about 30 min of
moderate activity
4. Stored in cells as highly concentrated, dark-staining, irregular granules
23
24
Polysaccharides
• Starch is a plant product

made of glucose polymer;
mixture of 2 different
polymers (amylose &
amylopectin).
Starch - Plants bank their surplus chemical energy in form of starch (potatoes &
cereals are primarily starch):
1. Amylose - unbranched, helical molecule; sugars joined by α(1—>4) linkages
2. Amylopectin - branched (less than glycogen with irregular branching pattern);
α(1—>6) bonds at branch.
3. Starch stored as densely packed granules (starch grains) found in membrane-
bound plastids within plant cells
4. Animals possess enzyme (amylase) to hydrolyze starch even though they don't
synthesize it
25
26
Polysaccharides
Cellulose: plant product
made of unbranched
polymers
• tough, durable structural
material (cotton, linen);
major plant cell wall
component
Cellulose:
1. Long, unbranched polymer of glucose units joined by β(1—>4)
2. Its properties differ dramatically from the above polysaccharides because of the
difference in bonds joining the glucose units.
3. Most multicellular organisms lack enzyme to degrade it.
4. Organisms that digest it (termites, sheep) harbor bacteria & protozoa that make
needed cellulase
27
Source: http://bio1151.nicerweb.com/Locked/media/ch05/cellulose.html

28
29
30
Polysaccharides
• Chitin: component of invertebrate

exoskeleton
• Unbranched polymer of N-
acetylglucosamine (acetyl amino
group instead of OH on glucose C2)
Chitin
1. Occurs widely as structural material among invertebrates (outer covering of insects,
spiders, crustaceans)
2. Tough, resilient yet flexible; similar to certain plastics; insects owe much of their
success to this highly adaptive polysaccharide covering

31
Acetyl amino
N-acetylglucosamine
group instead
of OH on
glucose C2

32
33
Polysaccharides
• Glycosaminoglycans (GAGs):
➢ Composed of repeating disaccharides (two different sugars; -A-B-A-B-A-B-), usually one is
an amino sugar.
➢ Found in extracellular space.

34
Activity
In groups:
Fill in the provided table:
Precursor(s) Polymer Type of

Polysaccharide Source (Branched/ Bonds Function
(Plant/ unbranched
Animal)
Glycogen
Starch
a-Amylose
b-Amylopectin
Cellulose
Chitin
GAGs

35
Lipids


36
Lipid
Lipids are a diverse group of nonpolar molecules whose common

properties are:
• Their ability to dissolve in organic solvents, such as chloroform or
benzene
• Their inability to dissolve in water.

37
Fats and fatty acids
• Lipids are a diverse group of nonpolar molecules. Lipids of importance in

cellular function include fats, oils, steroids, and phospholipids.
– Triacylglycerol (also called a triglyceride: e.g. 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.
38
• 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 structure of steroids. The phospholipid phosphatidylcholine.

39
Lipid
Triacylglycerol (triglyceride)
– Fats and oils are made of glycerol linked by three ester
bonds to three fatty acids (FA).

40
Lipid
• fatty acids (FA) are unbranched hydrocarbons with one

carboxyl group
• The two ends of a FA molecule have a very different structure,
they also have different properties:
– The hydrocarbon chain is hydrophobic, whereas the carboxyl group
(—COOH), which bears a negative charge, is hydrophilic.
– Molecules having both hydrophobic and hydrophilic regions are said
to be amphipathic.

41
FAs differ from one another in:

1- The length of their hydrocarbon chain
• Fatty acids present in cells typically vary in length from 14 to 20 carbons.

42
FAs differ from one another in:
2- The presence or absence of double bonds.
• 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.

43
• Tristearate, whose fatty acids lack double bonds, is a
common component of animal fats and remains in a
solid form.

44
Naturally occurring fatty acids have double bonds in the cis
configuration.
Double bonds (of the cis configuration) produce kinks in a fatty
acid chain.
• Consequently, the more double bonds that fatty acid chains
possess, the less effectively these long chains can be packed
together. This lowers the temperature at which a fatty acid-
containing lipid melts.
45
Function
Fats are very rich in chemical energy:
– a gram of fat contains over twice the energy content of a
gram of carbohydrate.
• Carbohydrates function primarily as a short-term,
rapidly available energy source
• Fat reserves store energy on a long-term basis.

46
• Because they lack polar groups, fats are
extremely insoluble in water and are stored in
cells in the form of dry lipid droplets.
• Since lipid droplets do not contain water as do
glycogen granules, they represent an
extremely concentrated storage fuel.

47
• In many animals, fats are stored in special cells
(adipocytes)
– Cytoplasm is filled with one or a few large lipid
droplets.
• Adipocytes exhibit a remarkable ability to
change their volume to accommodate varying
quantities of fat.

48
Steroids
• Steroids are four-ringed animal lipids that have been implicated in
atherosclerosis.
One of the most important

steroids is Cholesterol, a
component of animal cell
membranes and a precursor for
the synthesis of a number of
steroid hormones, such as:
– testosterone,
– progesterone, and
– estrogen
The structure of steroids.

49
Phospholipids
Phospholipids are a major component of cell membranes.
• The molecule resembles a

fat (triacylglycerol), but
has only two fatty acid
chains; it is a
diacylglycerol.
• The third hydroxyl of the
glycerol backbone is
covalently bonded to a
phosphate group,
The phospholipid phosphatidylcholine.
• which in turn is covalently
bonded to a small polar
group, such as choline
50
Phospholipids
• Thus, unlike fat molecules,
phospholipids contain two
ends that have very
different properties:
– the end containing the
phosphate group has a
distinctly hydrophilic
character;
– the other end composed of
the two fatty acid tails has a
distinctly hydrophobic
character.
The phospholipid phosphatidylcholine.
• Phospholipids are
amphipathic lipids

51
Proteins


52
• What is a Protein? Learn about the 3D shape
and function of macromolecules
https://www.youtube.com/watch?v=qBRFIMcxZ
NM
• And/Or
https://www.youtube.com/watch?v=wvTv8TqW
C48

53
Proteins
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.
54
Proteins
• As enzymes, proteins accelerate the rate of metabolic reactions.

• Structural roles, proteins provide mechanical support both within
cells and outside their perimeters.
• Hormones, growth factors, and gene activators.
• Membrane receptors and transporters, proteins determine what
a cell reacts to and what types of substances enter or leave the
cell.
• Contractile filaments and molecular motors, proteins constitute
the machinery for biological movements.
• Act as antibodies, serve as toxins, form blood clots, absorb or
refract light, and transport substances from one part of the body
to another.
55
Proteins
How can one type of molecule have so many varied

functions?
• Due to unlimited molecular structures that proteins, as a
group, can assume.
• Proteins have shapes and surfaces that allow them to
interact selectively with other molecules.
56
Proteins
The Building Blocks of Proteins:
Amino acids have an α carbon, an
amine group, a carboxyl group, and a
variable R group.

57
Proteins
With the exception of glycine, the α-carbon of amino

acids bonds to four different groups so that each amino
acid can exist in either a D or an L form.

58
Proteins
• What is the difference between them?
• Which isomer used for protein synthesis?

59
Proteins
• Amino acids are linked together by peptide bonds into a
polypeptide chain to make a protein.
• Peptide bond forms by dehydration reaction.
• Peptide bonds form between the carbonyl and the
amino of participating amino acids.

60
Proteins
• A polypeptide chain composed of a string of

amino acids joined by peptide bonds has the
following backbone:

61
Activity
In Groups:
1) Identify the number of amino acid residues

incorporated in the above polypeptide chain.
2) How many peptide bonds are there?

62
Activity
In Groups:
3) Match your answers.

63
Proteins
• Amino acids incorporated into a polypeptide chain
are termed residues.
• The residue on one end of the chain, the N-terminus,
contains a free (unbonded) -amino group,
• whereas the residue at the opposite end, the C-
terminus, has a free -carboxyl group.
N-terminus C-terminus

64
Proteins
• Many proteins contain other components that

are added after the polypeptide is
synthesized.
• These include carbohydrates (glycoproteins),
metal-containing groups (metalloproteins) and
organic groups (e.g., flavoproteins).

65
Proteins
• Amino acids differ in the R
group attached to one of the
bonds of the α-carbon.
– R groups may be polar
charged; polar
uncharged; nonpolar.

66
Proteins
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
active sites due to its ability gain or lose a proton in physiologic
pH ranges
67
arginine

68
B. Polar uncharged - R groups weakly acidic or basic;
partially charged at pH 7; can form H bonds with other
molecules like water since they have atoms with a partial
negative or positive charge
These amino acids are often quite reactive.

69
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
70
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 (α-helix)

71
D. The other three – glycine, proline, cysteine
3. Cysteine – R group has reactive —SH; forms disulfide (—
S—S—) bridge with other cysteines often at some distance
away in polypeptide backbone

72
Proteins
• R groups may have other properties.

– Glycine has only –H as its R
group and is small.
– The α-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.
Formation of disulfide bonds:
oxidation and reduction of bonds
between two cysteine residues

73
The Structure of Proteins
– Primary structure, the sequence of amino acids in the polymer, is critical to
the protein function.
N-terminus
C-terminus

74
– Primary structure: A linear sequence of amino

acids linked tighter by peptide bonds.
– The arrangement of amino acids in a chain is
genetically determined.
– The shape of protein is specified by its amino
acid sequence.

75
– Secondary structure refers to the conformation of
adjacent amino acids into α-helix, β-sheet.
– Result from hydrogen-bonding between the N-H and
C=O groups in the polypeptide backbone, without
involving the side chains.
The a-helix The b-pleated sheet

76
Alpha (α) helix:

twisting spiral
The backbone lies on the
inside of the helix, and
the side chains project
outward.
The a-helix

77
Alpha (α) helix:
•A H-bond is made between every
fourth peptide bond, linking the
N-H of one peptide bond to the
C=O group of another.
•Each turn of the helix comprises
3.6 amino acids residues.
The a-helix

78
β-Pleated sheet
The b-pleated sheet
– polypeptide lying side by side.
– The pleats result from the location of the α-carbons above and
below the plane of the sheet.
– Successive R groups project upward and downward from the
backbone.
– A -pleated sheet consists of a number of strands that lie
parallel to one another and are joined together by hydrogen
bonds between the carbonyl and imine groups of the
neighboring backbones. 79
The b-pleated sheet
β-Pleated sheet
• Neighboring segments of the polypeptide backbone may lie
either parallel (in the same N-terminal S C-terminal direction) or
antiparallel (in the opposite N-terminal S C-terminal direction).

80
Anti-parallel
β-pleated
sheet
Parallel β-
pleated sheet

81
• Those portions of a
polypeptide chain not
organized into helix or sheet
may consist of hinges, turns,
loops, or fingerlike
extensions.
• Often, these are the most
flexible portions of a
polypeptide chain and the
sites of greatest biological
activity.

82
Types of non-covalent
Ribbon model of bonds maintaining the
ribonuclease conformation of proteins
• 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.

83
• Fibrous proteins
– have an elongated shape,
– Structural proteins outside living cells are fibrous proteins,
such as collagens and elastins of connective tissues,
keratins of hair and skin, and silk.
– These proteins resist pulling or shearing forces to which
they are exposed.
• Globular proteins
– Have a compact shape.
– Most proteins within the cell are globular proteins.

84
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.

85
Proteins are
made up of
domains that
can be
conserved.
Dynamic movements within the

enzyme acetylcholinesterase.
• Protein Domains
– 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.

86
Dimer: TGF-b2
Hemoglobin: a and b globin Cysteine residues
Hydrophobic residues
• Quaternary structure refers to proteins
composed of subunits.
– It refers to the manner in which subunits
interact.
• Protein-Protein Interactions
– Different proteins can become physically
associated to form a multiprotein Pyruvate dehydrogenase:
complex. 60 polypeptide chains
87
Protein–protein interactions:
complementary molecular surfaces of
portions of two interacting proteins

88
• What is protein folding?
https://www.youtube.com/watch?v=yZ2aY5lxEG
E

89
• Watch the movie related to

Anfinsen Experiment in Protein
Folding:
https://www.youtube.com/watch?v=
tTNH6EVB_0w
Ribonuclease A
(RNase: 124 aa; 4 disulfide bonds)

90
• 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 agents
could lead to refolding.
Denature:
- 8M urea (unfold)
- b-mercaptoethanol: converts S-S to
sulfhydryl (—SH) groups
Ribonuclease A - Reversibility of events
(RNase: 124 aa; 4 disulfide bonds) - Information of the final 3D
conformation contained within the
primary sequence

91
The Human Perspective:
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, PrPc.
– CJD brains have PrPSc, which is identical or similar to PrPc but is
misfolded.
– “Mad cow disease”, kuru, and scrapie are also caused by PrPSc.

92
The Human Perspective:
Protein Misfolding Can Have Deadly Consequences
• Alzheimer’s 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 Aβ42, a protein that misfolds and self-associates into
amyloid plaques.
93
• 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

94
Nucleic acids


95
• 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 and
– Nucleotides are connected by 3’- nucleotide strands
5’ phosphodiester bonds of RNA
between the phosphate of one
nucleotide and the 3’ carbon of
the next.

96
• 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

97
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.

98
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99

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Chapter 2 The Structure and Functions of Biological Molecules, Biols300

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CHAPTER 2

The Structure and Functions of

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

• Define the chemical principles that form the basis of

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

• Understanding cellular function requires knowledge of

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

• Carbon is central to the chemistry of life.

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

• Functional groups—groups of atoms giving organic molecules

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

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

1. Carbohydrates include simple

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

An overview of the types of

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

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

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

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

Formation of an a- and b-pyranose

Monosaccharaides Disaccharides Oligosaccharides Polysaccharides

Glucose Sucrose Raffinose Glycogen

Fructose Lactose Stachyose Starch

Galactose Maltose Chitin

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

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

Polysaccharides: identical sugar monomers but dramatically different properties

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

• Disaccharides are used as a

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

Polysaccharides: identical sugar monomers but dramatically different properties

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

Polysaccharides: identical sugar monomers but dramatically different properties

• Cellulose, chitin, and glycosaminoglycans (GAGs): structural

• Glycogen is an animal product

1. Branches every 10 or so units; sugar at branch joined to 3 neighboring units

• Starch is a plant product

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

• Chitin: component of invertebrate

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

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

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

Precursor(s) Polymer Type of

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

An overview of the types of

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

Lipids are a diverse group of nonpolar molecules whose common

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

Fats and fatty acids

• Lipids are a diverse group of nonpolar molecules. Lipids of importance in

The structure of steroids. The phospholipid phosphatidylcholine.

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

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

• fatty acids (FA) are unbranched hydrocarbons with one

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

FAs differ from one another in:

• Fatty acids present in cells typically vary in length from 14 to 20 carbons.

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

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

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

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

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

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