Characteristics of Proteins Protein Function

Size of Proteins • Proteins perform crucial roles in all

• Proteins are very large polymers of biological processes.
amino acids with molecular weights 1. Catalytic function: Nearly all reactions
that vary from 6000 amu to several in living organisms are catalyzed by
million amu. proteins functioning as enzymes.
– Glucose (C6H12O6) = 180 amu Without these catalysts, biological
reactions would proceed much more
– Hemoglobin (C2952H4664O832N812S8Fe4) = 65,000 slowly.
2. Structural function: In animals
Molecular Number of Amino structural materials other than
Protein Weight (amu) Acid Residues inorganic components of the skeleton
are proteins, such as collagen
Insulin 6,000 51 (mechanical strength of skin and bone)
and keratin (hair, skin, fingernails).
Cytochrome c 16,000 104
3. Storage function: Some proteins
Growth hormone 49,000 191 provide a way to store small molecules
Rhodopsin 38,900 348 or ions, e.g., ovalbumin (used by
embryos developing in bird eggs),
Hemoglobin 65,000 574 casein (a milk protein) and gliadin
(wheat seeds), and ferritin (a liver
Hexokinase 96,000 730 protein which complexes with iron
ions).
Gamma globulin 176,000 1320
4. Protective function: Antibodies ar
Myosin 800,000 6100 proteins that protect the body from
amu disease by combining with and
Size of Protein destroying viruses, bacteria, and other
• Proteins are too large to pass through cell foreign substances. Another protective
membranes, and are contained within function is blood clotting, carried out
the cells where they were formed by thrombin and fibrinogen.
unless the cell is damaged by disease 5. Regulatory function: Body processes
or trauma. regulated by proteins include growth
– Persistent large amounts of protein (growth hormone) and thyroid
functions (thyrotropin).
in the urine are indicative of
damaged kidney cells. 6. Nerve impulse transmission: Some
– Heart attacks can also be proteins act as receptors for small
molecules that transmit impulses
confirmed by the presence of
certain proteins in the blood that across the synapses that separate nerve
are normally confined to cells in cells (e.g., rhodopsin in vision).
heart tissue. 7. Movement function: The proteins
Acid Base Properties actin and myosin are important in
• Proteins take the form of muscle activity, regulating
zwitterions. They have the contraction of muscle fibers.
characteristic isoelectric points, and 8. Transport function: Some
can behave as buffers in solutions. proteins bind small molecules or
ions and transport them through
• The tendency for large molecules to the body.
remain in solution or form stable
colloidal dispersions depends on the – Serum albumin is a blood protein
repulsive forces acting between that carries fatty acids between fat
molecules with like charges on their (adipose) tissue and other organs.
surfaces. – Hemoglobin carries oxygen from
– When proteins are at a pH in which the lungs to other body tissues.
there is a net positive or negative – Transferrin is a carrier of iron in
charge, the like charges cause the blood plasma.
molecules to repel one another, and • A typical human cell contains 9000
they remain dispersed. different proteins; the human
– When the pH is near the isoelectric body contains about 100,000
point, the net charge on the molecule different proteins.
is zero, and the repulsion between Classification by Structural Shape
proteins is small. This causes the Proteins can be classified on the basis of
protein molecules to clump and their structural shapes:
precipitate from solution. • Fibrous proteins are made up of long
rod-shaped or stringlike molecules that
 can intertwine with one another and
form strong fibers.
2. Salt bridges are attractions between
ions that result from the interactions of
– insoluble in water the ionized side chains of acidic amino
– major components of connective acids (—COO-) and the side chains of
basic amino acids (—NH3+).
tissue, elastic tissue, hair, and skin
– e.g., collagen, elastin, and keratin.
3. Hydrogen bonds can form between a
variety of side chains
• Globular proteins are more spherical in Hydrogen bonding also influences the secondary
shape structure, but here the hydrogen bonding is
– dissolve in water or form stable between R groups, while in secondary
suspensions. structures it is between the C=O and NH
– not found in structural tissue but portions of the backbone.
are transport proteins, or proteins 4. Hydrophobic interactions result from
that may be moved easily through the attraction of nonpolar groups, or
the body by the circularoty system when they are forced together by their
mutual repulsion of the aqueous
– e.g., hemoglobin and transferrin. solvent. These interactions are
36 particularly important between the
Classification by Composition benzene rings in phenylalanine or
Proteins can also be classified by tryptophan. This type of interaction is
composition: relatively weak, but since it acts over
large surface areas, the net effect is a
• Simple proteins contain only amino strong interaction.
acid residues. 4. cont. The compact structure of globular
• Conjugated proteins also contain other proteins in aqueous solution, in which
the nonpolar groups are pointed
organic or inorganic components,
called prosthetic groups. inward, away from the water
molecules.
– nucleoproteins — nucleic acids This changes the shape of red blood cells that carry
(viruses). this mutation to a characteristic sickle shape, which
– lipoproteins — lipids (fibrin in causes the cells to clump together and wedge in
blood, serum lipoproteins) capillaries, particularly in the spleen, and cause
– glycoproteins — carbohydrates excruciating pain.
(gamma globulin in blood, mucin • Cells blocking capillaries are rapidly
in saliva) destroyed, and the loss of these red
blood cells causes anemia.
– phosphoproteins — phosphate Protein Hydrolysis and Denaturation
groups (casein in milk)
• Amides can be hydrolyzed under acidic
– hemoproteins — heme or basic conditions.
(hemoglobin, myoglobin,
cytochromes)
• The peptide bonds in proteins can be
broken down under acidic or basic
– metalloproteins — iron (feritin, conditions into smaller peptides, or all
hemoglobin) or zinc the way to amino acids, depending on
the hydrolysis time, temperature, and
(alcohol dehydrogenase)
pH
Tertiary Structure of Proteins prote in + H2O H+ or OH
- smaller
• The tertiary structure of a protein peptides H+ or OH-
amino acids
refers to the bending and folding
of the protein into a specific three- – The digestion of proteins
dimensional shape. involves hydrolysis reactions
catalyzed by digestive
• These structures result from four enzymes.
types of interactions between the
R side chains of the amino acids – Cellular proteins are constantly
residues: being broken down as the body
resynthesizes molecules and
1. Disulfide bridges can form between tissues that it needs.
two cysteine residues that are close to Denaturation
each other in the same chain, or
between cysteine residues in different • Proteins are maintained in their native
chains. These bridges hold the protein state (their natural 3D conformation)
chain in a loop or some other 3D by stable secondary and tertiary
shape. structures, and by aggregation of
subunits into quaternary structures.
 milk; the proteins in the egg and milk
bind to the metal ions, forming a
precipitate, which is either vomited out
or pumped out.

Substance or condition Effect on Proteins

Disrupt hydrogen bonds and ionic attractions by

Heat and ultraviolet light making molecules vibrate too violently; produce
coagulation, as in cooking an egg

Organic solvents (ethanol

and others miscible with Disrupt hydrogen bonds in proteins and probably form
water) new ones with the proteins

Disrupt hydrogen bonds and ionic attractions; prolonged

Strong acids or bases
exposure results in hydrolysis of protein

Disrupt hydrogen bonds, hydrophobic interactions, and

Detergents
ionic attractions.

Heavy-metal ions (Hg2+, Ag+, Form bonds to thiol groups and precipitate proteins as
and Pb2+) insoluble heavy-metal salts
Denaturation is caused when the folded
native structures break down because
of extreme temps. or pH values, which
disrupt the stabilizing structures. The
structure becomes random and
disorganized.
• Most proteins are biologically active
only over a temperature range of 0ºC to
40ºC.
• Heat is often used to kill
microorganisms and deactivate their
toxins. The protein toxin from
Clostridium botulinum is inactivated
by being heated to 100ºC for a few
minutes; heating also deactivates the
toxins that cause diphtheria and
tetanus.
• Heat denaturation is used to prepare
vaccines against some diseases. The
denatured toxin can no longer cause the
disease, but it can stimulate the body to
produce substances that induce
immunity.
• Proteins can also be denatured by heavy-
metal ions such as Hg2+, Ag+, and Pb2+
that interact with —SH and carboxylate
groups.
– Organic materials containing Hg
(mercurochrome and merthiolate)
were common topical antiseptics.
– Heavy-metal poisoning is often treated
with large doses of raw egg white and