Title: Temperature-Dependent NMR and CD Spectra ofβ-Peptides: On the Thermal Stability ofβ-Peptide Helices - Is the Folding Process ofβ-Peptides Non-cooperative?
Abstract: Helvetica Chimica ActaVolume 82, Issue 1 p. 1-11 Research Article Temperature-Dependent NMR and CD Spectra of β-Peptides: On the Thermal Stability of β-Peptide Helices – Is the Folding Process of β-Peptides Non-cooperative? Karl Gademann, Karl Gademann Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorBernhard Jaun, Bernhard Jaun Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorDieter Seebach, Dieter Seebach Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorRemo Perozzo, Remo Perozzo Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this authorLeonardo Scapozza, Leonardo Scapozza Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this authorGerd Folkers, Gerd Folkers Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this author Karl Gademann, Karl Gademann Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorBernhard Jaun, Bernhard Jaun Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorDieter Seebach, Dieter Seebach Laboratorium für Organische Chemie der Eidgenössischen Technischen Hochschule, ETH-Zentrum, Universitätstrasse 16, CH-8092 ZürichSearch for more papers by this authorRemo Perozzo, Remo Perozzo Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this authorLeonardo Scapozza, Leonardo Scapozza Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this authorGerd Folkers, Gerd Folkers Department of Pharmaceutical Chemistry, ETH-Zürich, Winterthurerstrasse 190, CH-8057 ZürichSearch for more papers by this author First published: 19 January 1999 https://doi.org/10.1002/(SICI)1522-2675(19990113)82:1<1::AID-HLCA1>3.0.CO;2-NCitations: 55 Partially presented in a conference poster, see [1]. Part of the projected Ph. D. theses of K.G. and R.P., ETH-Zürich. AboutPDF 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 onFacebookTwitterLinked InRedditWechat Abstract Temperature-dependent NMR and CD spectra of methanol solutions of a β-hexapeptide and of a β-heptapeptide at temperatures between 298 and 393 K are reported. They establish the fact that the 314-helical secondary structures of the two β-peptides, 1 and 2, do not `melt' in the temperature range investigated. This is in sharp contrast to the behavior of the helices of α-peptides and proteins which undergo cooperative unfolding (`denaturing') upon heating. A non-cooperative mechanism is proposed, with a stepwise, rather than an `un-zipping' opening of H-bonded rings (cf. Fig. 6). The experimental results are regarded as evidence that, of the three effects which have been identified as contributing to the stability of β-peptide helices, i.e., H-bonding, hydrophobic interactions, and ethane staggering, the latter one is predominant. Citing Literature Volume82, Issue1January 13, 1999Pages 1-11 RelatedInformation
Publication Year: 1999
Publication Date: 1999-01-13
Language: en
Type: article
Indexed In: ['crossref']
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Cited By Count: 51
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