ANTIGEN ANTIBODY INTERACTION BONDS

MCQs-

1.The bonds involved in antigen-antibody interactions are

a) weak hydrogen bonds and vanderwalls forces

b) strong covalent bonds

c) strong di- sulphide bonds

d) all of these

Ans. a

2.Binding of antigen to antibody:

A.   Is usually unaffected by molecular rigidity. 

B. Is unaffected by the presence or absence of water molecules.
C.  Involves covalent bonding.
D.   Is optimized by spatial complementarity.

Ans. D Spatial complementarity is vital for strong binding of antigen to antibody otherwise non-specific intermolecular forces which depend reciprocally on distance apart, can become really strong.

3.The intermolecular forces which contribute to the interaction between antibody and antigen:

 A  Are all electrostatic.
 B  Are all vanderWaals.
 C  Are all hydrophobic.
 D  Are all hydrogen bonds.
 E  Rely on a combination of the above.

Ans.E Antibody–antigen interactions depend upon a combination of intermolecular forces, all of which are non-covalent.

Note-
1.The typical length of a hydrogen bond in water is 197 pm. 
2.The atom that looses the electron acquires positive charge and the other atom which gains the electron becomes a negatively charged particle. 
3.Vanderwall forces are weak forces of attraction between molecules. These forces decrease as the molecule gets smaller and increase as the molecule increases. 

Vanderwalls force ~molecular size 

Thank you for visiting my video tutorial /blog.Please feel free to share your comment on this

article ,Please subscribe and share the articles to get more such articles.