PROTEINS [111623]

Q2-LECTURE 1 \ Sir Galagates (ADV. BIO)

3. Aspartic Acid – major role in metabolism,

PROTEINS plays a role in hormone production and for
normal nervous system function.
- Composed of Carbon, Hydrogen, Oxygen, & 4. Glutamic Acid – important for protein
Nitrogen (CHON) synthesis
- Proteins help build and repair tissues and 5. Glutamine – for biosynthesis of proteins
muscles. 6. Asparagine – involved in nerve and brain
- Amino acids are the building tissue function
blocks/monomers of proteins. There are 20 7. Histidine – for growth and tissue repair
Amino acids.
8. Serine – needed for fat metabolism, muscle
- Of the 20, there are 9 essential amino acids.
growth
Essential Amino Acids – are those that the body 9. Threonine – for normal growth, maintain
cannot produce and are therefore taken from the protein balance
foods that we eat.

The 9 Essential Amino Acids: PROTEIN STRUCTURE

1. Histidine
2. Isoleucine The basic functioning of cells is entirely dependent
3. Leucine upon the structure of their proteins. The gene, or
4. Lysine sequence of DNA, determines the unique sequence
5. Methionine of amino acids in each peptide chain.
6. Phenylalanine
A change in nucleotide sequence of the gene’s
7. Threonine
coding region may lead to a different amino acid
8. Tryptophan
being added to the growing polypeptide chain,
9. Valine
causing a change in protein structure and therefore a
Complete Proteins – contain adequate proportion change in function.
of all nine essential amino acids necessary for the
dietary needs of humans and other animals.
1. PRIMARY STRUCTURE
The primary structure of a protein refers to
THE 20 AMINO ACIDS the sequence of amino acids in the
polypeptide chain. The primary structure is
 Charged: Arginine (Arg), Lysine (Lys).
held together by peptide bonds that are
Aspartic Acid (Asc), Glutamic Acid (Glu)
made during the process of protein
 Polar: Glutamine (Gln). Asparagine (Asn),
biosynthesis An average protein has 300
Histidine (His), Serine (Ser), Theronine (Thr),
amino acids
Tyrosine (Tyr), Cysteine (Cys), Methionine
(Met), Trytophan (Trp)
2. SECONDARY STRUCTURE
 Hydrophobic: Alanine (Ala), Isoleucine (Ile),
Leucine (Leu), Phenylalanine (Phe), Valine It is due to the interactions, like coiling or
(Val), Proline (Pro), Glycine (Gly) folding, of a polypeptide chain, using weak
hydrogen bonds, that gives protein its 3D
Functions of Amino Acids: shape.
1. Arginine – is converted into nitric oxide a. Alpha Helix Structure –
which helps blood vessels to relax and resembles a coiled spring and is
expand. secured by hydrogen bonding in
2. Lysine – concentrated in muscle tissue and the polypeptide chain. The length
helps in the absorption of calcium from the of the helix is determined by
intestinal tract, promotes bone growth. certain amino acids that will not
participate in these structures.
 Some proteins are made of several polypeptide
b. Beta Pleated Sheet – appears to subunits. (E.g. hemoglobin) It contains 4 subunits; 2
be folded or pleated held alpha and beta subunits
together by hydrogen bond
between polypeptide units that lie
adjacent to one another.

Protein Kinase C

CLASSIFICATION OF PROTEINS
Alpha Helix Structure of DNA is more stable than
Beta Pleated Sheet Structure.  Based on Structure
- Fibrous Proteins
- Globular Proteins
3. TERTIARY STRUCTURE - Intermediate Proteins
The Comprehensive 3D structure of the  Based on Composition
polypeptide chain of a protein. Several types of - Simple Proteins
bonds and forces hold a protein in its tertiary - Conjugated Proteins
structure namely; hydrophobic interactions,  Based on Functions
hydrogen bond, ionic bond, disulfide bridge - Structural Proteins, Enzymes,
(cysteine-cysteine bond), van der Waals forces Hormones
(distance-dependent). Secondary Structures fold - Pigments, Transport Proteins,
on themselves to form the tertiary structure of the Contractile Proteins
protein. - Storage Proteins, Toxins

3 Classes of Proteins Based on Structure:

1. Fibrous Proteins
- Are typically elongated and
insoluble.
- Involved in structure: tendons,
ligaments, blood clots (e.g. collagen
in connective tissues like tendons
and ligaments, keratin in hair, nails,
feathers, horns, claws, fibrin in blood
Chain B of Protein Kinase C clots.
- Contractile Proteins in movement:
muscle, microtubules, cytoskeleton,
mitotic spindle, cilia, and flagella like
actin and myosin.

2. Globular Proteins
- Are generally compact, soluble, and
spherical in shape.
- Most proteins which move around
MIL1 Protein (e.g. ovalbumin in egg, casein in
milk)
- Proteins with binding sites:
enzymes, hemoglobin,
4. QUARTENARY STRUCTURE
 immunoglobulins (antibodies), 2. Marasmus – The loss of body fat & muscle.
membrane receptor proteins Worst result of Anorexia Nervosa (eating
disorder).
3. Intermediate Proteins
- Are Intermediate filaments (Ifs),
Microfilaments (MFs), and
Microtubules (MTs) are the key
structural proteins that form the
cytoskeleton.

2 Classes of Proteins Based on Composition:

1. Simple Proteins
- Composed of only amino acids (e.g.
Albumins, Globulins, Collagen)

2. Conjugated Proteins
- Contain permanently associated
chemical groups (called as
prosthetic group) in addition to
amino acids.
- E.g. glycoproteins, nucleoproteins,
lipoproteins, phosphoproteins.

8 Proteins Classified Based on Function

1. Catalytic – enzymes (amylase, glucose,
lipase, pepsin, trypsin, ATPase, sucrose)
2. Storage – ovalbumin in eggs, casein in
milk, zein in maize
3. Transport – hemoglobin, carrier proteins in
cell membrane.
4. Communication – hormones (e.g. insulin,
glucagon, FSH, growth hormone,
neurotransmitters.)
5. Contractile – actin, myosin, dynein in
microtubules
6. Protective – immunoglobulin, fibrinogen,
fibrin (blood clotting factors)
7. Toxins – snake venom
8. Structural – cell membrane proteins,
keratin (hair), collagen, fibroin in silk.

LEVEL OF MALNUTRITION

1. Kwashiorkor (Ga language of Ghana) – the

sickness the baby gets when the new baby
comes; also called disease of a deposed
child. It is due to inadequate protein intake
and also known as edematous
malnutrition.