It is now generally accepted that the specificity of antibody is consequent to its amino acid sequence and mediated through the effects of sequence on the conformation of the combining site. Evidence for this has been obtained from reversible denaturation experiments on specific antibodies (Haber, 1964; Whitney and Tanford, 1965; Freedman and Sela, 1966) and has been inferred from comparisons of amino acid compositions of purified antibodies (Koshland, 1966), as well as from sequence studies on myeloma proteins (Hilschman and Craig, 1965; Titani et al., 1966; Milstein, 1966). Myeloma proteins have provided an excellent model for the study of antibody structure. These studies have revealed the regions of sequence common to all globulins of a given class as well as regions which are unique to each member. In this way they have pointed to the portions of the molecule which are likely to be responsible for forming the antibody combining...
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Haber et al. (1967) studied this question.