PROTEINS

Definition:
Proteins are complex nitrogenous substances of high molecular weight made up of chains of
alpha-amino acids joined by peptide bonds.
Protein is derived from Greek work “proteios” which means “of first importance” or “pre-
eminence”.

General Features:

 They are the fundamental constituents of living cells yet the most complex.
 They are essential to the growth and repair of all tissues.
 Proteins give the different tissues a sort of biological specificity.
 Plants can synthesize proteins from simple inorganic substances found in air and soil, but
animals depend largely on organic sources for their potential needs.
 Aside from C, H, O, and N other elements present in nearly all proteins are S and P.

Classifications:

A. According to Physical Structure

1. Globular (spherical) – compact proteins such as egg albumin, casein, most enzymes, and
antibodies.
2. Fibrous – stringy, elongated proteins such as collagen, silk fibroin, and keratin.

B. According to Function
1. Structural Proteins – more than half of the total protein of the mammalian body is
collagen, found in cartilages, tendons, and bones.
2. Contractile Proteins – examples are myosin and actin found in skeletal muscles.
3. Protective Proteins – examples are the keratins of hair, nails, wool, scales, feather,
hoofs, horns, and skin. Leather is almost pure keratin.
4. Transport Protein – example is hemoglobin.
5. Catalytic Proteins – examples are enzymes.
6. Regulatory Proteins – examples are peptide hormones such as insulin, growth hormone,
etc.
7. Antibodies – example is immunoglobulin.

C. According to Composition
1. Derived Proteins – produced from simple and conjugated protein upon the action of
heat, acids, alkalis, and enzymes.
a. Primary derived proteins - proteins which have undergone slight intermolecular
rearrangement thru the action of certain physical or chemical agents. They are
also called denatured proteins. They are insoluble in water.
Examples:
 Proteans – first products produced by the action of acids, enzyme, or
water. Ex. Edestan derived from edestin
 Metaproteins – produced by the further action of acid or alkali.
 Coagulated proteins – produced by the action of heat or alcohol.

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 b. Secondary derived proteins – mixtures of fragments of original proteins varying
in size. Products of further hydrolysis of proteins.
Examples: in order of decreasing complexity
 Proteoses
 Peptones
 Peptides

2. Simple Proteins –
TYPE: Solubility Action Special note Examples
in water of heat
Albumins Sol. Coag. Ppt. w/ sat (NH4)2SO4 Ovalbumin,
Not ppt. w/ NaCl Serum albumin
Histones Sol. Sol. in dil. acid Blood corpuscles
Insol. in ammonia of birds.
Protamines Sol. Sol. in dil. acid and Sturin & salmin in
ammonia sperm of fish
Globulins Coag. Ppt. w/ sat (NH4)2SO4 Serum globulin,
ppt. w/ NaCl ovoglobulin,
myosin, edestin
Glutelins Coag. Insol in dil. Neutral Glutenin (wheat),
salt but sol. in dil. Acid oryzenin (rice)
and alkali
Prolamines Sol. In 60 to 80% EtOH Gliadin (wheat),
zein (corn)
Scleroproteins Highly insoluble Elastin (tendon),
(albuminoid) keratin & fibroin

3. Conjugated Proteins – these are simple proteins in combination with non-protein

groups.
a. Phosphoproteins – Casein in milk, and vitellin in egg yolk
b. Glycoproteins – Mucin in saliva
c. Chromoproteins – Hemoglobin and myoglobin
d. Nucleoproteins – Nuclein
e. Lipoproteins – Chylomicron, HDL, and LDL

AMINO ACIDS
 the building blocks of proteins
 General formula R–CH–COOH or H2N–CH–OOH
ӏ ӏ
NH 2 R
 Amphoteric
 Contain chiral carbon (except Glycine)

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Amino acids are classified according to R group
1. Nonpolar side chain R group name / structure Other name / IUPAC
a. Glycine Hydrogen

b. Alanine Methyl

c. Valine Isopropyl

d. Leucine Isobutyl

e. Isoleucine Sec-butyl

f. Phenyl alanine Phenylmethyl

g. Tryptophan Indol

h. Methionine Methylthioethyl

i. Proline α–pyrrolidine

2. Uncharged polar side chain R group name / structure Other name / IUPAC
a. Serine Hydroxymethyl

b. Threonine 1-hydroxyethyl

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 c. Tyrosine p-hydroxyphenylmethyl

d. Cysteine Thiomethyl

e. Asparagine Methyl amide

f. Glutamine Ethyl amide

3. Acidic side chain R group name / structure Other name / IUPAC

a. Aspartic acid Ethanoic acid

b. Glutamic acid Propanoic acid

4. Basic side chain R group name / structure Other name / IUPAC

a. Lysine n-butylamine

b. Arginine n-propyl guanido

c. Histidine imidazole

LEVELS OF STRUCTURE OF PROTEIN

1. Primary Structure
 Refers to the number and sequence of amino acids in its polypeptide chain.
 Stabilized by peptide bond.
2. Secondary Structure
 Refers to the fixed conformation of the polypeptide backbone.
 Stabilized by intermolecular hydrogen bond.

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 o Alpha helix – responsible for the coiled structure.
o Beta-pleated sheet – responsible for the folded structure.
3. Tertiary Structure
 This is the unique three dimensional structure of each protein unit.
 Stabilized by hydrogen bond, salt bridge, disulfide linkage and hydrophobic interaction.
4. Quaternary Structure
 Refers to the structure formed from the union of at least two protein subunits.
 Stabilized by the same kind of forces that are involved in maintaining the tertiary
structure.