Antigen-antibody recognition. Model calculations

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 noti...

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Veröffentlicht in:	Biophysical chemistry 1994-08, Vol.51 (2), p.337-347
Hauptverfasser:	Nauchitel, Vladimir V., Somorjai, Rajmund L.
Format:	Artikel
Sprache:	eng
Schlagworte:	Accessibility Amino Acid Sequence Amino Acids - chemistry Animals Antibody Antigen Antigen-Antibody Complex - chemistry Binding Sites Chemical Phenomena Chemistry, Physical Hydrophobicity Immunoglobulin Fab Fragments - chemistry Models, Chemical Molecular Sequence Data Muramidase - chemistry Muramidase - immunology Proteins Recognition Residues Thermodynamics
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Zusammenfassung:	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.
ISSN:	0301-4622 1873-4200
DOI:	10.1016/0301-4622(94)00054-9