Antigen-antibody recognition. Model calculations.

V V Nauchitel; R L Somorjai

doi:10.1016/0301-4622(94)00054-9

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PubMed · 7919042

Antigen-antibody recognition. Model calculations.

V V Nauchitel·R L Somorjai

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Abstract

Free energy of antigen-antibody binding has been calculated for HyHEL-5, HyHEL-10, and D1.3 complexes. We also have calculated free energies of binding per residue of L- and H- chains of the antibodies, and those of the antigen (lysozyme). The results of the calculations provide support for the notion that TYR and TRP residues may confer on the CDRs of antibodies an enhanced capacity for binding antigens. It was shown also that the composition of residues that provide major part of the binding free energy differs for antibodies and antigens.

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Amino Acid Sequence Amino Acids Animals Antigen-Antibody Complex Binding Sites Chemical Phenomena Chemistry, Physical Immunoglobulin Fab Fragments Models, Chemical Molecular Sequence Data Muramidase Thermodynamics Journal Article

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V V Nauchitel, R L Somorjai. 1994. Antigen-antibody recognition. Model calculations.. https://doi.org/10.1016/0301-4622(94)00054-9

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