AMINO ACIDS

Amino acids are group of organic

compounds containing two functional groups
– and .
General structure
Classification of amino acids
• According to polarity
I. Non-polar amino acid have no charge on
the “R” group
 Polar amino acids
Neutral amino acids carry no
charge on the “ R” group
Polar, neutral amino acids
Basic amino acids
Acidic polar amino acids
 Essential amino acids
cannot be synthesized by the body and,
need to be supplied through the diet.
Arginine Valine
Histidine Leucine
Isoleucine Lysine
Methionine Phenylalanine
Threonine Tryptophan
 Non-essential amino acids
The body can synthesize about 10
amino acids to meet not be
consumed in the diet.
Glycine Alanine
Serine Cysteine
Aspartate Asparagine
Glutamate Glutamine
Tyrosine Proline
Classification based on their
metabolic fate
Glycogenic amino acids can serve
as precursors for the formation of
glucose or glycogen.
Alanine
Aspartate
Glycine
Methionine
Ketogenic amino acids. Fat can
be synthesized from these
amino acids.
Leucine
Lysine
 Glycogenic and
ketogenic amino acids
Isoleucine
Phenylalanine
Tryptophan
Tyrosine
PROPERTIES OF AMINO ACIDS
Solubility. Most of amino acids
are soluble in water and insoluble in
organic solvents.
Melting point. Amino acids
generally melt at higher
O
temperature, often above 200 C.
Optical properties
 Optical properties
The α-carbon of an amino acid is attached to
four different chemical groups (asymmetric) and
is, a chiral, or optically active carbon atom.
Amino acids with an asymmetric center at the
α-carbon can exist in two forms: D and L, that
are mirror images of each other
• Zwitterion or dipolar ion. Amino acids
in solution at neutral pH exist as dipolar ions,
meaning that the proton on the carboxyl
group has migrated to the amino group.
• Isoelectric pH is defined as the pH at
which a molecule exist as a zwitterion or
dipolar ion and carries no net charge. Thus,
the molecule is electrically neutral.
 Amino acids as ampholytes
• A zwitterion acts as an acid (proton donor):

• A zwitterion acts as a base (proton acceptor):

PROTEINS
 Functions of proteins
• Structural proteins provide
mechanical support: keratin of
hair, nail, collagen of bone.
• Enzymes and catalytic proteins
accelerate rate of biochemical
reaction in the human body.
Transport proteins carry materials
from one place to another in the
body.
Hemoglobin and myoglobin
transport and storage of O2.
Plasma albumin transports free
fatty acids, bilirubin, steroid
hormones, calcium.
Regulatory proteins (hormones)

Control metabolism and cell

reproduction.
Insulin lowers blood glucose
level
Glucagon elevates blood
glucose level
• Contractile proteins: myosin
and actin take part in the muscle
contraction.
• Storage proteins: Ovalbumin
of eggs and casein of milk source
of amino acids for development of
fetus.
• Genetic proteins: nucleoproteins
take part in transmission of
genetic information.
• Defense proteins or antibodies
which are produced by the
immune system in response to
antigens. Antigens are bacteria
and viruses.
The peptide bond is formed between the α
– carboxyle group of one amino acid and
the α-amino group of another amino acid
with releasing of water .
 Structural organization of
protein molecule
Primary structure is the linear sequence of
amino acids in the chain are joined by the
peptide bond.
• The primary structure of proteins is
dictated by the genetic information in
the DNAs.
• Secondary structure results from folding
of the covalently linked amino acids into
regularly repeating structure.
 Tertiary structure is the further
folding of a peptide to a globular
structure.
The chemical bonds that maintain
tertiary structure
 The nature of chemical bonds
that maintain tertiary structure
• a) ionic bond
• b) hydrogen bond
• C) hydrophobic interactions
• D) dipol-dipol interactions
Tertiary structure of myoglobine
• Quaternary structure is the
association of two or more
peptide chains to form the
functional protein.
Structure of insulin
• Hemoglobin (Hb) is a tetramer
composed of 2α-subunits and
2β-subunits.
 Properties of proteins

• 1. Solubility: Proteins form colloidal

solution due to huge size of protein
molecule.
• 2. Molecular weight: Proteins has high
molecular weight.
• 3. Proteins are ampholytes due to
presence of NH2 – and - COOH groups.
• 4. Isoelectric pH. At isoelecrtic pH, the
proteins exist as zwitterions or dipolar
ions. They are electrically neutral with
minimum solubility, maximum
precipitability and least buffering
capacity. The isoelectric pH for some
proteins: Pepsine-1.1; Casein - 4.6;
Albumin – 4.7; hemoglobin - 6.7.
•
When net electric charge of the proteins is
zero they no longer repeal one another. As
a result, they clump together and
precipitate out of solution.
 Denaturation is
disorganization of native
protein structure. It results in
the loss of secondary, tertiary
and quaternary structure of
proteins. It doesn’ t alter the
primary structure.
Renaturation is regeneration of
native protein structure after
removing denaturating agent.
Denaturation and renaturation
Agents of denaturation
 Temperature
Increasing the temperature increases the
rate of molecular movement, and the bonds
within the proteins begin to vibrate more
violently. As a result the weak interactions,
like hydrogen bonds and hydrophobic
interactions are disrupted. The protein
molecules are denatured as they lose their
characteristic three dimensional
conformation and become completely
disorganized.
 If the body temperature becomes too
high, or if local regions of the body are
subjected to very high temperatures, as
when you touch a hot cookie sheet,
cellular proteins become denatured.
They lose their function, and the cell or
the organism dies.
 Mechanical Stress
Stirring, whipping, or shaking can
disrupt the weak interactions that
maintain protein conformation.
 pH.
R groups of the amino acids, all proteins
have a characteristic electric charge. The
positively and negatively charged R groups
on the surface of the molecule interact with
ions and water molecules, and these
interactions keep the protein in solution
within the cytoplasm. Changing pH alter the
net charge on the protein, causing
electrostatic repulsion and the disruption of
some hydrogen bonding.
When the blood pH drops too low, blood
proteins become polycations. Similarly,
when the blood pH rises too high, the
proteins become polyanions. In either
case, the proteins will unfold because
of charge repulsion and loss of
stabilizing ionic interactions.
 Under these extreme conditions, the
denatured blood proteins wouldn’ t be able to
carry out their functions. The blood cells would
also die as their critical enzymes were
denatured. The hemoglobin in the red blood
cells would become denatured and wouldn’ t
be able to transport oxygen.
Fortunately, the body has a number of
mechanisms, such as the carbonate buffer
system, to avoid the radical changes in the
blood pH that can occur as a result of
metabolic or respiratory difficulties.
 Organic Solvents
Polar organic solvent, denature proteins
by disrupting hydrogen bonds within the
protein, in addition to forming hydrogen
bonds with the solvent, water. The
nonpolar regions of these solvents
interfere with hydrophobic interactions
in the interior of the protein molecule,
thereby disrupting the conformation.
 Heavy Metals
Heavy metal ions 2+
(Pb , 2+
Hg , 2+
Cd ) denature
protein by attacking the ̶ SH groups. They form
- 2+ -
salt bridges, as in S ̶ Hg ̶ S .
This very feature is taken advantage of in the
antidote for heavy metal poisoning: raw egg
whites and milk. The egg and milk proteins are
denatured by the metal ions, forming insoluble
precipitates in the stomach. These must be
pumped out or removed by inducing vomiting.
Classification of proteins
based on their shapes
 SHAPE OF PROTEINS
Fibrous proteins Globular proteins
• Fiber like in shape • Spherical in shape
• Insoluble in water • Soluble in water or other
• Resistant to digestion. solvents
• Collagen, keratin, • Digestible
elastin. • Hemoblobin, myoglobin,
albumin
 Nutritional classification
Complete proteins have all the ten essential
amino acids in the required proportion by the
body to promote good growth. e.g. egg
ovalbumin, milk casein.
Partially incomplete proteins are partially
lacking one or more essential amino acids and
hence can promote moderate growth. Wheat
and rice proteins (limiting Lys, Thr).
Incomplete proteins: lack one and more
essential amino acids and they do not promote
growth at all e.g. gelatin lacks Trp, corn’ s zein
lacks Trp and Lys.
Classification of proteins
based on chemical nature
 Simple proteins
• Glutelins and prolamines are mostly
found in plants e.g. glutelin (wheat), zein
(mice).
• Histones and protamines are strongly
basic proteins and they are found in
association with nucleic acids.
• Albumins and globulins are plasma
proteins.
 Electrophoresis of plasma proteins

The total concentration of plasma proteins is 6-8 g/dl

 Plasma albumin functions
• Osmotic pressure: Due to its high
concentration and low molecular weight,
albumin contributes to 75-80% of the total
plasma osmotic pressure. Thus, albumin takes
part in maintaining blood volume and body
fluid distribution.
• Transport function: Plasma albumin
transports free fatty acids, billirubin, steroid
hormones, calcium and copper (10%).
• Nutritive functions: Albumin serves as a
source of amino acids for tissue protein
synthesis to a limited extend, particularly
in nutritional deprivation of amino acids.
• Buffering function: Among the plasma
proteins, albumin has the maximum
buffering capacity.
 Globulins
• α1- globulins takes part in the transport of
carbohydrates and lipids. They are protein
parts of glycoproteins and lipoproteins.
• α2 – globulins protein part of ceruloplasmin,
which responsible for transport of copper.
• β – globulins is protein part of transferrin.
Transferrin is a transporter of iron in the
circulation.
• γ- globulins are protein parts of
immunoglobulins namely IgG, IgA, IgM, IGD
and IGE.
 Conjugated proteins
Chromoproteins: are conjugated
proteins in which the prosthetic group is
colored pigment.
Flavoproteins the prosthetic group is
vitamin B2 derivatives FAD and FMN.
They are yellow color.
Hemeproteins are a group of
conjugated proteins that contain heme
as a prosthetic group (red color).
Nucleoproteins are conjugated proteins that
contain nucleic acids as a prosthetic group.
Glycoproteins: the prosthetic group is
carbohydrates.
Phosphoproteins: Phosphoric acid is the
prosthetic group.
Metalloproteins: the prosthetic group is Me ions:
Ferritin’ s function is storage of iron.
Transferrin transports iron.
Ceruloplasmin transports copper.
 Lipoproteins
Chylomicrons - they are synthesized in the
intestine and transports exogenous (dietary)
lipids to various tissues.
Very low density lipoproteins (VLDL). They are
produced in liver and are responsible for the
transport of endogenously synthesized
triglycerols.
Low density lipoproteins (LDL). They are formed
from VLDL in the blood circulation. They transport
cholesterol from liver to other tissues.
High density lipoproteins (HDL). HDL transports
cholesterol from peripheral tissues to liver
(reverse cholesterol transport).