By Frank J. Dixon (Eds.)
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Additional resources for Advances in Immunology
1984). , 1985a,b); the most highly protruding convex regions have the fewest intramolecular packing interactions, hence, the most flexibility and the most chemical interactions immediately available to an antibody. To analyze the complex immune response to intricate antigens such as proteins, one can use either defined antibodies or defined antigens to select individual specificities. In a complementary approach to the use of selective antibodies (monoclonal technology), selective antigens (peptide homologs of the protein sequence) have been used to define the ANTIBODY BINDING TO PROTEIN ANTIGENS 29 individual specificities within polyclonal anti-MHr antisera.
Smith-Gill, and D. R. Davies) from X-ray diffraction studies of these antibodies in antibody-lysozyme complexes (H. M. Geysen and S. J. Smith-Gill, unpublished results). Although preliminary, the peptide mapping results identified the unpublished HyHELlO site and correctly suggested the involvement of Trp and Arg in the complex. , 1982). In principle, the characterization of critical residues, originally studied by peptide mapping and comprehensive single-residue substitution in peptides (see Sections IV and V), can be done in the context of the native protein fold, using cloning and site-directed mutation methods.
Continuing this trend, the plot of solvent-exposed surface area (Fig. 8) shows more of a minimum near hexapeptide 54 (a reactivity peak) than hexapeptide 30 (a reactivity minimum). , 1986). However, this trend does not continue: the most antigenic residues do not have more exposed surface area per residue than those with average antigenicity. 5. 04). The ratio of main-chain to side-chain surface area is similar for positions with most and average reactivity and lower for the least reactive positions.