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Science 6 March 1987:
Vol. 235. no. 4793, pp. 1184 - 1190
DOI: 10.1126/science.3823878
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Articles

Science, Vol 235, Issue 4793, 1184-1190
Copyright © 1987 by American Association for the Advancement of Science

articles

Chemistry of antibody binding to a protein

HM Geysen, JA Tainer, SJ Rodda, TJ Mason, H Alexander, ED Getzoff, and RA Lerner

The chemistry of antibody recognition was studied by mapping the antigenicity of the protein myohemerythrin with peptide homologs of the protein sequence. The results suggest that the entire protein surface is antigenic, but the probability of there being antibodies to a given site is influenced by local stereochemistry. Although accessible to an antibody binding domain, the least reactive positions cluster in the most tightly packed and least mobile regions and are closely associated with narrow, concave grooves in the molecular surface containing bound water molecules. The most frequently recognized sites form three-dimensional superassemblies characterized by high local mobility, convex surface shape, and often by negative electrostatic potential.


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