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An analysis of the helix-to-strand transition between peptides with identical sequence

2000; Wiley; Volume: 41; Issue: 2 Linguagem: Inglês

10.1002/1097-0134(20001101)41

1097-0134

Xianghong Jasmine Zhou, Frank Alber, Gerd Folkers, Gastón H. Gonnet, Gareth Chelvanayagam,

Chemical Synthesis and Analysis

Proteins: Structure, Function, and BioinformaticsVolume 41, Issue 2 p. 248-256 Research Article An analysis of the helix-to-strand transition between peptides with identical sequence Xianghong Zhou, Xianghong Zhou Department of Computer Science, Eidgenössische Technische Hochshule, Zürich, Switzerland Department of Applied Bioscience, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorFrank Alber, Frank Alber International School for Advanced Studies (SISSA) and Istituto Nazionale di Fisica della Materia (INFM), Trieste, ItalySearch for more papers by this authorGerd Folkers, Gerd Folkers Department of Applied Bioscience, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorGaston H. Gonnet, Gaston H. Gonnet Department of Computer Science, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorGareth Chelvanayagam, Corresponding Author Gareth Chelvanayagam [email protected] Department of Computer Science, University of Western Australia, Perth, AustraliaDepartment of Computer Science, The University of Western Australia, Stirling Highway, Nedlands, Perth, W.A., 6009, Australia===Search for more papers by this author Xianghong Zhou, Xianghong Zhou Department of Computer Science, Eidgenössische Technische Hochshule, Zürich, Switzerland Department of Applied Bioscience, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorFrank Alber, Frank Alber International School for Advanced Studies (SISSA) and Istituto Nazionale di Fisica della Materia (INFM), Trieste, ItalySearch for more papers by this authorGerd Folkers, Gerd Folkers Department of Applied Bioscience, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorGaston H. Gonnet, Gaston H. Gonnet Department of Computer Science, Eidgenössische Technische Hochshule, Zürich, SwitzerlandSearch for more papers by this authorGareth Chelvanayagam, Corresponding Author Gareth Chelvanayagam [email protected] Department of Computer Science, University of Western Australia, Perth, AustraliaDepartment of Computer Science, The University of Western Australia, Stirling Highway, Nedlands, Perth, W.A., 6009, Australia===Search for more papers by this author First published: 24 August 2000 https://doi.org/10.1002/1097-0134(20001101)41:2 3.0.CO;2-JCitations: 34Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract An analysis of peptide segments with identical sequence but that differ significantly in structure was performed over non-redundant databases of protein structures. We focus on those peptides, which fold into an α-helix in one protein but a β-strand in another. While the study shows that many such structurally ambivalent peptides contain amino acids with a strong helical preference collocated with amino acids with a strong strand preference, the results overwhelmingly indicate that the peptide's environment ultimately dictates its structure. Furthermore, the first naturally occurring structurally ambivalent nonapeptide from evolutionary unrelated proteins is described, highlighting the intrinsic plasticity of peptide sequences. We even find seven proteins that show structural ambivalence under different conditions. 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