PROTEINS SERVE MANY FUNCTIONS, INCLUDING THE CHIRALITY OF a-AMINO ACIDS

FOLLOWING:
• With the exception of glycine, all protein-
1. Structure: Collagen and keratin are the chief derived amino acids have at least one
constituents of skin, bone, hair, and nails. stereocenter (the a-carbon) and are chiral.
• The vast majority of a-amino acids have the L-
2. Catalysts: Virtually all reactions in living systems are
configuration at the a-carbon.
catalyzed by proteins called enzymes.

3. Movement: Muscles are made up of proteins called

myosin and actin.

4. Transport: Hemoglobin transports oxygen from the

lungs to cells, other proteins transport molecules
across cell membranes. • Figure 22-2 A comparison of the configuration
of L-alanine and D-glyceraldehyde (as
5. Hormones: Many hormones are proteins, among Fischer projections):
them insulin, oxytocin, and human growth hormone.

6. Protection: Blood clotting involves the protein

fibrinogen; the body used proteins called antibodies to
fight disease.

7. Storage: Casein in milk and ovalbumin in eggs store

nutrients for newborn infants and birds. Ferritin, a
protein in the liver, stores iron.

8. Regulation: Certain proteins not only control the • Human basically use 20 amino acids to make
expression of genes, but also control when gene any type of protein
expression takes place.

PROTEINS ARE DIVIDED INTO TWO TYPES:

• Fibrous proteins – insoluble in water,

structural purposes
• Globular proteins – more or less soluble in
water, non-structural purposes

AMINO ACIDS WHAT ARE ZWITTERIONS?

Amino acid: A compound that contains both an amino
group and a carboxyl group.
a-Amino acid: An amino acid in which the amino group
is on the carbon adjacent to the carboxyl group.
Proline – has a bond between R an N
R groups – determine polarity
Non-polar – hydrophobic
• Zwitterion - compounds that have a positive
charge on one atom and a negative charge on
another
- zwitter meaning “hybrid”
• An amino acid has –COOH and –NH2 groups in
the same molecule. Therefore, in water
solution, the –COOH donates a proton to the –
NH2 so that an amino acid actually has the
structure:

Polar – (neutral, acidic, basic) hydrophilic

• All proteins in the body are the L-isomer. D-

Amino acids are extremely rare in nature (cell
walls of a few types of bacteria).
• Acidic solution: acid donates a proton to -COO
group, turning your zwitterion into a positive
ion (cation)
 • Basic solution: causes the -NH3+ to donate its PROTEIN DERIVED a-AMINO ACIDS
proton to OH, turning the zwitterion into a
• Nonpolar side chains: Each ionizable group is
negative ion (anion)
shown in the form present in highest
• If the amino acid is a positive ion at low pH, and
concentration at pH 7.0).
a negative ion at high pH, there must be some
pH at which the molecules have equal positive
and negative charges – isoelectric point
• Amphiprotic – compound that is both an acid
and a base
• Buffer solution – solution that neutralizes both
acid and base

IONIZATION VS. pH

• The net charge on an amino acid depends on

the pH of the solution in which it is dissolved.
• If we dissolve an amino acid in water, it is
• Polar side chains (at pH 7.0)
present in the aqueous solution as its
zwitterion.
• If we add a strong acid such as HCl to bring the
pH of the solution to 0.0, the strong acid
donates a proton to the -COO- of the
zwitterion turning it into a positive ion.

• If we add a strong base such as NaOH to the • Acidic and base side chains (at pH 7.0)
solution and bring its pH to 14, a proton is
transferred from the NH3+ group to the base
turning the zwitterion into a negative ion.

• To summarize:

• For 19 of the 20, the a-amino group is primary;

ISOELECTRIC POINT • For proline, it is secondary.
• With the exception of glycine, the a-carbon of
• Isoelectric point, pI: The pH at which the each is a stereocenter.
majority of molecules of a compound in
• Isoleucine (left) and threonine (right) contain a
solution have no net charge.
second stereocenter.
Nonpolar & Acidic
polar side chains pI Side Chains pI
alanine 6.01 aspartic acid 2.77
asparagine 5.41 glutamic acid 3.22
cysteine 5.07
glutamine 5.65
glycine 5.97
isoleucine 6.02 Basic
leucine 5.98 Side Chains pI
methionine 5.74 arginine 10.76
phenylalanine 5.48 histidine 7.59
proline 6.48 lysine 9.74
serine 5.68
threonine 5.87
tyrosine 5.66
tryptophan 5.88
valine 5.97
CYSTEINE (CYS, C)
• The -SH (sulfhydryl) group of cysteine is easily
oxidized to an -S-S- (disulfide).
PHENYLALANINE (PHE, F), TRYPTOPHAN (TRP, W),
AND TYROSINE (TYR, Y)
• The amino acids phenylalanine, tryptophan,
and tyrosine have aromatic rings on their side
chains.
- Aromatic amino acids absorb
ultraviolet light at 280nm
• Tryptophan is the precursor to the
neurotransmitter serotonin (5-
hydroxytryptamine), has a calming effect
• Manic-depressive schizophrenia (bipolar
disorder) – managed by controlling levels of
serotonin
• Tyrosine – normally derived from
phenylalanine; converted to the class of
neurotransmitters called catecholamines,
epinephrine and adrenaline
• L-Dihydroxyphenylalanine (L-dopa) – - Found only in the thyroid gland
intermediate in the conversion of tyrosine to
epinephrine; decreased levels is associated
with Parkinson’s disease. Tyrosine and
phenylalanine supplements might increase
dopamine but L-dopa, the immediate
precursor is prescribed because it passes into
the brain quickly.
OTHER AMINO ACIDS
• Hydroxylation (oxidation) of proline, lysine,
and tyrosine, respectively and iodination for
tyrosine, give these uncommon amino acids.
• Proline → Hydroxyproline
• Lysine → Hydroxylysine
• Tyrosine → Thyroxine
• Other amino acids are derived from common
amino acids
• Produced by modification of the parent amino
acid after the protein is synthesized by an
organism through the process called post-
translational modification
• Hydroxyproline and hydroxylysine
- Have hydroxyl groups on their side
chains
- Found only in a few connective tissues
(collagen)
• Thyroxine
- Has an extra iodine containing
aromatic group
- Released as a hormone by hydrolysis
of thyroglobulin
- Helps ramp up metabolism
PEPTIDES
• In 1902, Emil Fischer proposed that proteins
are long chains of amino acids joined by amide
bonds.
• Peptide bond (peptide linkage): The special
name given to the amide bond between the a-
carboxyl group of one amino acid and the a-
amino group of another.
• Order of amino acids in a peptide or protein is
critical to both the structure and function
• Peptide: A short polymer of amino acids joined
by peptide bonds; they are classified by the
number of amino acids in the chain.
• Dipeptide: A molecule containing two amino
acids joined by a peptide bond.
• Tripeptide: A molecule containing three amino
acids joined by peptide bonds.
• Polypeptide: A macromolecule containing
many amino acids joined by peptide bonds.
• Protein: A biological macromolecule
containing at least 30 to 50 amino acids joined
by peptide bonds.
• The individual amino acid units are often
referred to as “residues”.