By Frank J. Dixon (Eds.)
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By using such replacement net data, each residue of a peptide was assigned to one of four descriptive categories : essential (irreplaceable), selected (selectively replaceable), partially replaceable, or generally replaceable. For example, in MHr site 4-9 (Fig. lOC), Ile-4 can be replaced by any of the other 19 commonly occurring amino acids, without affecting peptide binding by the antisera (generally replaceable). Similarly, Pro-5 can be replaced by most other amino acids without influencing antibody binding.
Curved arrows indicate plausible side-chain movements, when antibody binding to critical exposed polar side chains results in the breaking of one or more charged and/or hydrogen-binding interactions. Binding of the critical exposed Glu-6 side chain (red, top center) could disrupt the interaction with the Lys-100side chain (blue, right), which packs against and forms a gate to the surface for the buried T y r 8 side chain (yellow, center). (B) A postulated side-chain movement of Tyr leads to a resulting change in the antigenic surface topography.
1984). Before accepting a definition of antigenic residues as all those found in the interface with a n antibody, it is worth considering that the essence of antigenicity involves binding energy. In the broadest sense, two contrasting possibilities could account for the interaction energy of protein antigens: (1) the total binding energy encompasses numerous, small contributions from some 15 (the average number of residues suggested to constitute the interface in the 3 determined structures) or more interacting residues, such that any single amino acid contributes a relatively small portion of the energy and specificity to the chemistry of 24 ELIZABETH D.