6. What are the noncovalent forces holding the antigen antibody together? Describe.

The recognition of antigen by antibody involves noncovalent, reversible binding. Various types
of noncovalent interactions may contribute to antibody binding of antigen, including electrostatic
forces, hydrogen bonds, van der Waals forces, and hydrophobic interactions. The relative importance
of each of these depends on the structures of the binding site of the individual antibody and of the
antigenic determinant. The strength of the binding between a single combining site of an antibody and
an epitope of an antigen is called the affinity of the antibody. The affinity is commonly represented by
a dissociation constant (Kd), which indicates how easy it is to separate an antigen-antibody complex
into its constituents. A smaller Kd indicates a stronger or higher affinity interaction because a lower
concentration of antigen and of antibody is required for complex formation. The Kd of antibodies
produced in typical humoral immune responses usually varies from about 10-7M to 1O-11M. Serum
from an immunized individual will contain a mixture of antibodies with different affinities for the
antigen, depending primarily on the amino acid sequences of the CDRs.

Works Cited
(2007). Structural and Chemical Basis of Antigen Binding. In A. K. Abbas, A. H. Lichtman, &
S. PilIai, Cellular and Molecular Immunology Sixth Edition (p. 99). Philadelphia:
SAUNDERS Elsevier.