Академический Документы
Профессиональный Документы
Культура Документы
Longer polymer
Dehydration reaction in the synthesis of a polymer
Hydrolysis of a polymer
The Diversity of Polymers
Glyceraldehyde
Ribose
Glucose Galactose
Dihydroxyacetone
Ribulose
Fructose
• Monosaccharides serve as a major fuel for cells
and as raw material for building molecules
Dehydration
1–2
reaction in the glycosidic
synthesis of sucrose linkage
Glucose
monomer
Glycogen granules
in muscle
tissue Glycogen
Cellulose microfibrils
in a plant cell wall Cellulose
Cellulose
Hydrogen bonds
molecules
between —OH groups
(not shown) attached to
carbons 3 and 6
Storage Polysaccharides
1 µm
Amylose Amylopectin
0.5 µm
Glycogen
0.5 µm
Plant cells
Cellulose
molecules
Glucose
monomer
• Enzymes that digest starch by hydrolyzing alpha
linkages can’t hydrolyze beta linkages in cellulose
• Cellulose in human food passes through the
digestive tract as insoluble fiber
• Some microbes use enzymes to digest cellulose
• Many herbivores, from cows to termites, have
symbiotic relationships with these microbes
• Chitin, another structural polysaccharide, is found
in the exoskeleton of arthropods
• Chitin also provides structural support for the cell
walls of many fungi
• Chitin can be used as surgical thread
Lipids are a diverse group of hydrophobic
molecules
• Lipids are the one class of large biological
molecules that do not form polymers
• The unifying feature of lipids is having little or no
affinity for water
• Lipids are hydrophobic because they consist
mostly of hydrocarbons, which form nonpolar
covalent bonds
• The most biologically important lipids are fats,
phospholipids and steroids
Fats
Glycerol
Dehydration reaction in the synthesis of a fat
• Fats separate from water because water
molecules form hydrogen bonds with each
other and exclude the fats
• In a fat, three fatty acids are joined to
glycerol by an ester linkage, creating a
triacylglycerol, or triglyceride
Ester linkage
Structural
formula of a
saturated fat
molecule
Structural
formula
of an
unsaturated
Space-filling fat molecule
model of
stearic acid,
a saturated
fatty acid
Space-filling
model of oleic
acid, an
unsaturated
fatty acid Double bond
causes bending.
• Fats made from saturated fatty acids are called
saturated fats
• Most animal fats are saturated
• Saturated fats are solid at room temperature
• A diet rich in saturated fats may contribute to
cardiovascular disease through plaque deposits
Stearic acid
Choline
Phosphate
Glycerol
Hydrophobic tails
Fatty acids
Hydrophilic
head
Hydrophobic
tails
(a) Structural formula (b) Space-filling model (c) Phospholipid (d) Phospholipid
symbol bilayer
• When phospholipids are added to water, they self-
assemble into a bilayer, with the hydrophobic tails
pointing toward the interior
• The structure of phospholipids results in a bilayer
arrangement found in cell membranes
• Phospholipids are the major component of all cell
membranes
WATER
Hydrophilic
head
Hydrophobic
WATER
tails
Steroids
Glucose
Enzyme
(sucrose)
Fructose
Defensive proteins
Function: Protection against disease
Example: Antibodies inactivate and help
destroy viruses and bacteria.
Antibodies
Virus Bacterium
Storage proteins
Function: Storage of amino acids
Examples: Casein, the protein of milk, is
the major source of amino acids for baby
mammals. Plants have storage proteins
in their seeds. Ovalbumin is the protein
of egg white, used as an amino acid
source for the developing embryo.
Transport
protein
Cell membrane
Hormonal proteins
Function: Coordination of an organism’s
activities
Example: Insulin, a hormone secreted by
the pancreas, causes other tissues to
take up glucose, thus regulating blood
sugar concentration.
Insulin
High secreted Normal
blood sugar blood sugar
Receptor proteins
Function: Response of cell to chemical
stimuli
Example: Receptors built into the
membrane of a nerve cell detect signaling
molecules released by other nerve cells.
Receptor
protein
Signaling molecules
Contractile and motor proteins
Function: Movement
Examples: Motor proteins are responsible
for the undulations of cilia and flagella.
Actin and myosin proteins are
responsible for the contraction of
muscles.
Actin Myosin
Muscle tissue 30 m
Structural proteins
Function: Support
Examples: Keratin is the protein of hair,
horns, feathers, and other skin appendages.
Insects and spiders use silk fibers to make
their cocoons and webs, respectively.
Collagen and elastin proteins provide a
fibrous framework in animal connective
tissues.
Collagen
Connective tissue
60 m
Polypeptides
Amino Carboxyl
group group
Nonpolar side chains; hydrophobic
Side chain
(R group)
New peptide
bond forming
Side
chains
Back-
bone
helix
pleated sheet
Transthyretin Transthyretin
polypeptide protein
• Primary structure, the sequence of amino acids
in a protein, is like the order of letters in a long
word
• Primary structure is determined by inherited
genetic information
Primary structure
Amino
acids
1 5 10
Amino end
30 25 20 15
35 40 45 50
75
80 85 90
95
120 125
Carboxyl end
• The coils and folds of secondary structure result
from hydrogen bonds between repeating
constituents of the polypeptide backbone
• Typical secondary structures are a coil called an
alpha helix and a folded structure called a beta
pleated sheet
Secondary structure
helix
Hydrogen bond
pleated sheet
strand
Hydrogen
bond
Tertiary structure
Transthyretin
polypeptide
Hydrophobic
interactions and
van der Waals
interactions
Polypeptide
backbone
Hydrogen
bond
Disulfide bridge
Ionic bond
Quaternary structure
Transthyretin
protein
• Quaternary structure results when two or more
polypeptide chains form one macromolecule
• Collagen is a fibrous protein consisting of three
polypeptides coiled like a rope
• Hemoglobin is a globular protein consisting of
four polypeptides: two alpha and two beta chains
Polypeptide
chain Chains
Iron
Heme
Chains
Polypeptide chain Collagen Hemoglobin
Sickle-Cell Disease: A Simple Change in
Primary Structure
• A slight change in primary structure can affect a
protein’s conformation and ability to function
• Sickle-cell disease, an inherited blood disorder,
results from a single amino acid substitution in the
protein hemoglobin
10 µm 10 µm
Secondary
Primary Quaternary Red Blood Cell
and Tertiary Function
Structure Structure Shape
Structures
Normal Molecules do not
1 hemoglobin associate with one
2 another; each carries
3 oxygen.
Normal
4
5 subunit
6
7
5 m
3
4
5
6 subunit
7
5 m
What Determines Protein Conformation?
Renaturation
The Protein-Folding Problem
Hollow
cylinder
Chaperonin
(fully assembled)
Correctly
Polypeptide folded
protein
Diffracted X-rays
X-ray
X-ray
source
beam
Crystal
Nucleic acid Protein
X-ray
source X-ray
beam
Results
RNA DNA
RNA
polymerase
Nucleic acids store and transmit hereditary
information
• The amino acid sequence of a polypeptide is
programmed by a unit of inheritance called a gene
• Genes are made of DNA, a nucleic acid
The Roles of Nucleic Acids
Synthesis of
mRNA in the nucleus
mRNA
NUCLEUS
CYTOPLASM
mRNA
Movement of
mRNA into cytoplasm
Ribosome
via nuclear pore
Synthesis
of protein
Amino
Polypeptide acids
The Structure of Nucleic Acids
3C
Nucleoside
Nitrogenous
Cytosine (C) Thymine Uracil
base
(T, in DNA) (U, in RNA)
Purines
Phosphate
5C group Sugar
(pentose) Adenine (A) Guanine (G)
3C
(b) Nucleotide
Sugars
3 end
(a) Polynucleotide, or nucleic acid
Nucleoside
Nitrogenous
base
Phosphate
group Pentose
sugar
Nucleotide
3 end
Polynucleotide, or
nucleic acid
5 3 Sugar-phosphate
backbones
Hydrogen bonds
Purines
Adenine Guanine
A G
Pentose sugars
Nucleoside components
Nucleotide Polymers
Sugar-phosphate
backbone
Old strands
Nucleotide
about to be
added to a
new strand
5 end
New
strands
3 end 5 end
5 end 3 end
DNA and Proteins as Tape Measures of Evolution