{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,10,24]],"date-time":"2023-10-24T11:11:01Z","timestamp":1698145861872},"reference-count":23,"publisher":"Wiley","issue":"10","license":[{"start":{"date-parts":[[2004,2,1]],"date-time":"2004-02-01T00:00:00Z","timestamp":1075593600000},"content-version":"vor","delay-in-days":4140,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biopolymers"],"published-print":{"date-parts":[[1992,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The peptide YKGTMDSG (Tyr\u2010Lys\u2010Gly\u2010Thr\u2010Met\u2010Asp\u2010Ser\u2010Gly) represents an important antigenic determinant from the glycoprotein G2 of the pathogenic Rift Valley fever virus. By preparing a series of single\u2010residue substitution peptides, the importance to antigenicity of individual residues within this octapeptide has been determined. Here, we investigated a simple and rapid computational analysis to test for correlations between the observed antigenicity of the substitution analogue peptides and the calculated conformational preferences in local regions of the peptides. Conformational energy analyses were carried out on all dipeptide combinations represented in the wild\u2010type octapeptide and in the singleresidue substitution analogue peptides. Conformational similarities and differences between wild\u2010type and substitution dipeptide pairs were determined. The results of these computational analyses were then compared with the data on the relative antigenicity of the wild\u2010type octapeptide and the substitution analogues. This comparison revealed a positive correlation. Substitution peptides showing changes in antigenicity possessed significant changes in the calculated backbone conformation relative to wild type in the dipeptides encompassing the residue substitution. Substitution peptides showing no change in antigenicity similarly showed no significant changes in dipeptide conformation. The potential utility of dipeptide conformational energy analyses and this preliminary structure\u2010activity correlation are discussed. \u00a9 1992 John Wiley &amp; Sons, Inc.<\/jats:p>","DOI":"10.1002\/bip.360321013","type":"journal-article","created":{"date-parts":[[2004,12,30]],"date-time":"2004-12-30T02:44:36Z","timestamp":1104374676000},"page":"1407-1415","source":"Crossref","is-referenced-by-count":0,"title":["Dipeptide backbone conformation and antibody recognition of a viral octapeptide epitope"],"prefix":"10.1002","volume":"32","author":[{"given":"David C.","family":"Feller","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Marc S.","family":"Collett","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2004,2]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/0167-5699(87)90239-8"},{"key":"e_1_2_1_3_2","volume-title":"Synthetic Vaccines","author":"Arnon R.","year":"1987"},{"key":"e_1_2_1_4_2","first-page":"21","volume-title":"Contributions to Epidemiology and Biostatistics","author":"Peters C. J.","year":"1981"},{"key":"e_1_2_1_5_2","first-page":"321","volume-title":"The Biology of Negative Strand Viruses","author":"Collett M. S.","year":"1987"},{"key":"e_1_2_1_6_2","first-page":"371","volume-title":"Vaccines 89","author":"Dalrymple J. M.","year":"1989"},{"key":"e_1_2_1_7_2","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1128\/jvi.58.2.263-270.1986","volume":"58","author":"Keegan K.","year":"1986","journal-title":"J. Virol."},{"key":"e_1_2_1_8_2","first-page":"31","volume":"6","author":"Zimmerman S. S.","year":"1989","journal-title":"Comments Mol. Cell. 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