Biochemistry

Part - 4
By Dr.M.Shams…………………………………………………………..01002200666
 Bonds of protein Molecules

 Protein molecule is stabilized by 2 strong bonds (peptide and sulphur bonds) and 3 weak bonds (hydrogen, electrostatic and
hydrophobic bonds)

1-Peptide bond 2-Disulphide bond

 Formed by condensation between carboxyl  Formed between two cysteine residues of two parallel
group of an amino acid & amino group of the next amino polypeptides or two adjacent parts of the same polypeptide.
acid in polypeptide chain.
 3-Hydrogen bond 4-Hydrophobic bond 5-Electrostatic bond
(salt bridge)
Formed between carbonyl group (C-O) of one Weak forces that attract non polar Formed between oppositely charged
chain and amide group (-NH) of the other chain side chain of neutral amino acids. groups of side chains amino acids

Formed between phenyl rings of two Such as positive charges on amino

phenylalanine amino acids in which groups of basic amino acids and
the rings are stalk on each other negative charges on carboxyl groups
of acidic amino acids.
 Orders of protein structure
1- Primary structure

 The number and sequence of amino acids in polypeptide chain

 formed from amino acids connected together by peptide bond

2- Secondary structure

 This type is formed as a result of coiling of polypeptide chain to form helix.

 This helical structure is maintained by hydrogen and disulphide bonds.

3- Tertiary structure

 It is refer to the coiling of several helical portion of a single helix or several helixes into a three dimensional structure.
 The shape of protein at this level of organization is correlated with its biological function which may be globular or fibrous proteins

1. Fibrous proteins 2. Globular proteins

Has linear shape Has spherical shape
More stable Less stable
They have axial ratio more than 10 They have axial ratio less than 10
(axial ratio length/width of protein molecules)
e.g. keratin & myosin. e.g. albumin & globulins.

4- Quaternary structure

 This level is reached by aggregation of several tertiary subunits to form polymers.

 e.g. → Hemoglobin
 Properties of proteins
1- Solubility of proteins
 Each protein molecule has specific solubility at a certain pH and certain concentration of salt.

2- Precipitation of proteins
 Proteins are precipitated from solution by process is called deproteinization.
 Such precipitation reactions are important in
a) Isolation
b) Purification of proteins from mixtures.

These methods include:

1) Salting out: High concentration of neutral salts →ammonium sulphate & sodium sulphate.
2) Isoelectric point.
3) By organic solvents → e.g. alcohol or acetone.
4) By salts of heavy metals →e.g. silver nitrate and lead acetate.
5) By strong acids e.g. → tri-chloro-acetic acid.

3- Electrophoresis
 It is a migration of proteins in an electric field.
 Charged particles of protein will migrate to one electrode or to other one at rate that depends on
1. The net charge
2. the supporting medium
3. Molecular weight.
4- Buffering action of proteins:
 This is the property by which proteins are able to resist the change in the pH of their solution.
 This property is due to the presence of many ionic groups (+) and (-) charges → e.g. amino group (basic) & carboxyl group
(acidic)

5- Denaturation of proteins
 It is the change in physical, chemical and biological properties of proteins
 Denaturizing factors produce disruption of the weak forces → disrupt secondary, tertiary and quaternary structure of proteins.
 This effect does not cause destruction of peptide linkage.

Denaturizing factors include

I. Physical factors 2. Chemical factors
1) high temperature 1)strong acids
2) high pressure 2) strong alkalis
3) shaking 3) salts of heavy metals
4) x-rays and ultra violet rays. 4) organic solvents.

Effects of denaturation
A- Physical changes
1- Decreased solubility.
2- Decreased infusibility.
3- Increased viscosity.
B- Chemical changes C- Biological changes
1- Loss of hydrogen, hydrophobic and 1- 1. Loss of enzymatic, hormonal and other
electrostatic bonds biological properties of proteins.
2- Some chemical groups become exposed 2- Loss of antigenic activities.
like SH groups. 3- Denaturized proteins are easily digested.