Answer
The VL and VH domains of the immunoglobulins have similar homologous structures each of which consist of the beta-pleated sheets which are packed face to face order with the main chains of each of the domains about 10Aº apart and are inclined to an angle of -300. These beta pleated sheets of each of the domains are mainly linked to each other by a conserved disulfide bridge. The hypervariable loops are mainly located on the surface of these domains, this helps the loops to tolerate more of the amino acid substitutions. The V₁ and VH domains which are highly confined to the hypervariable loops thus is arranged so to tolerate more amino acid substitutions and the changes in the amino acids on beta pleated sheets could result in the destabilization of these domains.
Work Step by Step
The VL and VH domains of the immunoglobulins have similar homologous structures each of which consist of the beta-pleated sheets which are packed face to face order with the main chains of each of the domains about 10Aº apart and are inclined to an angle of -300. These beta pleated sheets of each of the domains are mainly linked to each other by a conserved disulfide bridge. The hypervariable loops are mainly located on the surface of these domains, this helps the loops to tolerate more of the amino acid substitutions. The V₁ and VH domains which are highly confined to the hypervariable loops thus is arranged so to tolerate more amino acid substitutions and the changes in the amino acids on beta pleated sheets could result in the destabilization of these domains.
