Proteins BSN

Proteins
Proteins
Introduction:
• Groups of organic compounds
• Polymers of amino acids
• Perform diverse functions in body
The term protein is derived from a Greek word proteios,
meaning holding the first place. Berzelius (Swedish chemist)
suggested the name proteins to the group of organic
compounds that are utmost important to life.
They are the most abundant organic molecules of the living
system. They occur in every part of the cell and constitute
about 50% of the cellular dry weight. Proteins form the
fundamental basis of structure and function of life.
Elemental composition of proteins:
• Carbon : 50 – 55%
• Hydrogen : 6 – 7.3%
• Oxygen : 19 – 24%
• Nitrogen : 13 – 19%
• Sulfur : 0 – 4%
Besides the above, proteins may also contain other
elements such as P, Fe, Cu, I, Mg, Mn, Zn etc. The
content of nitrogen, an essential component of
proteins, on an average is 16%.
Functions of Proteins
• Proteins
• Provide strength to the body
• Constituent of membrane structure
• Acts as enzymes
• Acts as hormones
• Acts as blood clotting factors
• Immunoglobulins
• Genetic control
• Muscle contraction
• Respiration
• Storage proteins
• Membrane receptors
Amino Acids
As many as 300 amino acids occur in nature— Of these, only 20—known as
standard amino acids are repeatedly found in the structure of proteins, isolated
from different forms of life— animal, plant and microbial. This is because of
the universal nature of the genetic code available for the incorporation of only
20 amino acids when the proteins are synthesized in the cells.
Definition:
Amino acids are a group of organic compounds containing two functional
groups— amino and carboxyl. The amino group (—NH2) is basic while the
carboxyl group (—COOH) is acidic in nature.
Nutritional classification of amino acids
Essential amino acids:

The amino acids which cannot be synthesized by the body and,
therefore, need to be supplied through the diet are called essential
amino acids. They are required for proper growth and
maintenance of the individual.
Non-essential amino acids:
The body can synthesize about 10 amino acids to meet the
biological needs, hence they need not be consumed in the diet.
Conditionally essential amino acids:
Normal healthy individual can synthesize all essential amino acids
but under pathophysiological conditions such as surgery, thermal
injury, wounds etc. body is unable to synthesize one or more
amino acids and ,hence it is required to consume these amino
acids through diet.
Essential amino Non essential amino Conditionally
acids acids essential amino acids
• Arginine • Glycine • Cysteine
• Valine • Alanine • Glycine
• Histidine • Serine • Glutamine
• Isoleucine • Cysteine
• Leucine • Aspartate
• Lysine • Asparagine
• Methionine • Glutamate
• Phenylalanine • Glutamine
• Threonine • Tyrosine
• Tryptophan • Proline
Classification of amino acids on polarity
• Hydrophilic
• Posses groups such as hydroxyl,
sulfhydryl, and amide groups
Polar amino acids which participate in hydrogen
bonding of protein structure.
• Glycine, Serine, threonine etc.
• Hydrophobic
• The non-polarity arises due to the
Non-polar amino presence of nonpolar side chains
acids or R-groups, such as methyl or
ethyl groups.
• Alanine, Leucine, Isoleucine etc.
Classification of proteins
Structure
Function
Classification of Proteins Composition
Solubility
Nutrition
Structural classification of
Proteins
Considering the structure proteins are classified into four types:
• Primary
• Secondary
• Tertiary
• Quaternary
Primary Structure:
It is the linear sequence of amino acids that forms the backbone of
proteins.
Secondary structure :
The spatial arrangement of protein by twisting of the polypeptide chain.
Tertiary structure :
The three dimensional structure of a functional protein.
Quaternary structure :
Some of the proteins are composed of two or more polypeptide chains
referred to as subunits. The spatial arrangement of these subunits is
known as quaternary structure.
Bonds in structures of proteins
Bonds present in primary structure:
The primary structure of proteins is held together by peptide bond.
Formation of peptide bond:
When the amino group of an amino acid combines with carboxyl group
of another amino acid, a peptide bond is formed.
Bonds present in secondary structure:
The amino acids are located close to each other in their
sequence. Two types of secondary structures, alpha-helix and
beta-sheet, are mainly identified.
The alpha-helix is a tightly packed coiled structure with
amino acid side chains extending outward from the central
axis. The alpha-helix is stabilized by extensive hydrogen
bonding. It is formed between H atom attached to peptide N,
and O atom attached to peptide C. The hydrogen bonds are
individually weak but collectively, they are strong enough to
stabilize the helix.
Beta-Pleated sheets are composed of two or more segments
of fully extended peptide chains. In the beta sheets, the
hydrogen bonds are formed between the neighboring
segments of polypeptide chain.
Bonds present in tertiary structure :
Besides the hydrogen bonds, disulfide bonds ( -S-S), ionic interactions
(electrostatic bonds), hydrophobic interactions contribute to the tertiary
structure of proteins.
Disulfide bond:
The disulfide bonds may be formed in a single polypeptide chain or
between different polypeptides. These bonds contribute to the structural
conformation and stability of proteins.
Hydrophobic interaction:
The occurrence of hydrophobic forces is observed in aqueous environment
wherein the molecules are forced to stay together.
Electrostatic interaction:
These bonds are formed by interactions between negatively charged groups
(e.g. COO–) of acidic amino acids with positively charged groups (e.g.
NH3 +) of basic amino acids.
Bonds present in Quaternary Structure:
The monomeric subunits are held together by non-covalent bonds namely
hydrogen bonds, hydrophobic interactions and ionic bonds.
Functional Classification of
Proteins
Structural proteins : Keratin of hair and nails, collagen
of bone.
 Enzymes or catalytic proteins : Hexokinase, pepsin.
 Transport proteins : Hemoglobin, serum albumin.
 Hormonal proteins : Insulin, growth hormone.
Contractile proteins : Actin, myosin.
 Storage proteins : Ovalbumin, glutelin.
 Genetic proteins : Nucleoproteins.
 Defense proteins : Snake venoms, Immunoglobulins.
Receptor proteins: for hormones, viruses.
Classification of protein according to solubility
Depending upon solubility proteins are classified into two types:

• Globular proteins : These are spherical or oval in shape,
soluble in water or other solvents and digestible.
• Examples of globular proteins:
Albumins, Globulins, Histones etc.
• Fibrous proteins : These are fiber like in shape, insoluble in

water and resistant to digestion. Albuminoids or scleroproteins
are predominant groups of fibrous proteins.
• Example of fibrous proteins:
Collagen, Elastin, Keratin etc.
Classification of proteins on composition
Proteins are broadly classified into 3 major groups on the basis of
composition:
1. Simple proteins : They are composed of only amino acid
residues.
2. Conjugated proteins : Besides the amino acids, these proteins
contain a non-protein moiety known as prosthetic group or
conjugating group.
3. Derived proteins : These are the denatured or degraded
products of simple and conjugated proteins.
Conjugated proteins:
(a) Nucleoproteins : Nucleic acid (DNA or RNA) is the
prosthetic group e.g. nucleohistones, nucleoprotamines.
(b) Glycoproteins : The prosthetic group is carbohydrate. e.g.
mucin (saliva), ovomucoid (egg white).
(c) Lipoproteins : Protein found in combination with lipids as the
prosthetic group e.g. serum lipoproteins.
(d) Phosphoproteins : Phosphoric acid is the prosthetic group
e.g. casein (milk), vitelline (egg yolk).
(e) Chromoproteins : The prosthetic group is coloured in nature
e.g. hemoglobins, cytochromes.
(f) Metalloproteins : These proteins contain metal ions such as
Fe, Co, Zn, Cu, Mg etc., e.g. ceruloplasmin (Cu), carbonic
anhydrase (Zn).
Nutritional Classification of
proteins
The nutritive value of proteins is determined by the composition
of essential amino acids. From the nutritional point of view,
proteins are classified into 3 categories.
1. Complete proteins : These proteins have all the ten essential
amino acids in the required proportion by the human body to
promote good growth. e.g. egg albumin, milk casein.
2. Partially incomplete proteins : These proteins partially lack
one or more essential amino acids, and can promote moderate
growth. e.g. wheat and rice proteins (limiting Lys, Thr).
3. Incomplete proteins : These proteins completely lack one or
more essential amino acids. Hence they do not promote growth at
all e.g. gelatin (lacks Trp).

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Proteins

Essential amino acids:

Classification of Proteins Composition

Depending upon solubility proteins are classified into two types:

• Fibrous proteins : These are fiber like in shape, insoluble in

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