ABSTRACT
Somatic mutation has been implicated as a significant and possibly primary factor in affinity maturation and memory in the humoral immune response. The rate of somatic mutation has been estimated to be as high as one point mutation per cell division. The mutability properties of the antibody repertoire are considered from a slightly different perspective in S. A. Kauffman et al., where the authors discuss somatic mutation in the context of an affinity landscape. X-ray crystallographic studies have shown that the binding site of an antibody appears as an irregularly shaped surface formed primarily by the amino acids that constitute the complementarity-determining regions of the variable heavy and light chains. The bond between an antigenic epitope and an antibody is the result of complex interactions between chemical functional groups on the surface of the antigen and amino-acid side groups in the binding site of the antibody.
