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 |
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| container_title | Biophysical chemistry |
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| creator | Nauchitel, Vladimir V. Somorjai, Rajmund L. |
| description | 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. |
| doi_str_mv | 10.1016/0301-4622(94)00054-9 |
| format | Article |
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It was shown also that the composition of residues that provide major part of the binding free energy differs for antibodies and antigens.</description><identifier>ISSN: 0301-4622</identifier><identifier>EISSN: 1873-4200</identifier><identifier>DOI: 10.1016/0301-4622(94)00054-9</identifier><identifier>PMID: 7919042</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>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</subject><ispartof>Biophysical chemistry, 1994-08, Vol.51 (2), p.337-347</ispartof><rights>1994 Elsevier Science B.V.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c357t-d08e3db1b8b061e5018ae1e8060032ed256f8ab9bb223573570d6fbf67cc5a2d3</citedby><cites>FETCH-LOGICAL-c357t-d08e3db1b8b061e5018ae1e8060032ed256f8ab9bb223573570d6fbf67cc5a2d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0301462294000549$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7919042$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nauchitel, Vladimir V.</creatorcontrib><creatorcontrib>Somorjai, Rajmund L.</creatorcontrib><title>Antigen-antibody recognition. 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It was shown also that the composition of residues that provide major part of the binding free energy differs for antibodies and antigens.</description><subject>Accessibility</subject><subject>Amino Acid Sequence</subject><subject>Amino Acids - chemistry</subject><subject>Animals</subject><subject>Antibody</subject><subject>Antigen</subject><subject>Antigen-Antibody Complex - chemistry</subject><subject>Binding Sites</subject><subject>Chemical Phenomena</subject><subject>Chemistry, Physical</subject><subject>Hydrophobicity</subject><subject>Immunoglobulin Fab Fragments - chemistry</subject><subject>Models, Chemical</subject><subject>Molecular Sequence Data</subject><subject>Muramidase - chemistry</subject><subject>Muramidase - immunology</subject><subject>Proteins</subject><subject>Recognition</subject><subject>Residues</subject><subject>Thermodynamics</subject><issn>0301-4622</issn><issn>1873-4200</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kFtLw0AQhRdRaq3-A4U-iT6kzl6ySV6EUrxBxRd9XvYyKStptmZTof_ejS0-CgMHZs6ZYT5CLinMKFB5BxxoJiRjN5W4BYBcZNURGdOy4JlgAMdk_Gc5JWcxfiYTlAAjMioqWoFgYwLztvcrbDOd1AS3m3Zow6r1vQ_tbPoaHDZTqxu7bfTQiufkpNZNxIuDTsjH48P74jlbvj29LObLzPK86DMHJXJnqCkNSIo50FIjxRIkAGfoWC7rUpvKGMZSIBU4WZtaFtbmmjk-Idf7vZsufG0x9mrto8Wm0S2GbVSFLLjgOUtGsTfaLsTYYa02nV_rbqcoqAGUGiiogYKqhPoFpaoUuzrs35o1ur_QgUya3-_nmJ789tipaD22Fp1PhHrlgv__wA-mVXY3</recordid><startdate>19940801</startdate><enddate>19940801</enddate><creator>Nauchitel, Vladimir V.</creator><creator>Somorjai, Rajmund L.</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19940801</creationdate><title>Antigen-antibody recognition. 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| ispartof | Biophysical chemistry, 1994-08, Vol.51 (2), p.337-347 |
| issn | 0301-4622 1873-4200 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_76734352 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 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 |
| title | Antigen-antibody recognition. Model calculations |
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