Importance of Ring Puckering versus Interstrand Hydrogen Bonds for the Conformational Stability of Collagen

Mismatch is fine: Proline derivatives with a ring pucker mismatching that of natural collagen but with favorable torsional angles along the peptide chain are readily tolerated within the collagen triple helix (see picture). In contrast, a competition between intramolecular and interstrand H bonds de...

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Bibliographic Details
Published in:	Angewandte Chemie International Edition Vol. 50; no. 30; pp. 6835 - 6838
Main Authors:	Erdmann, Roman S., Wennemers, Helma
Format:	Journal Article
Language:	English
Published:	Weinheim WILEY-VCH Verlag 18-07-2011 WILEY‐VCH Verlag Wiley Subscription Services, Inc
Edition:	International ed. in English
Subjects:	Animals cis/trans amide bonds collagen Collagen - chemistry Humans Hydrogen Bonding Models, Molecular PPII helix proline Proline - chemistry Protein Conformation Protein Denaturation protein engineering Protein Stability Protein Structure, Secondary Thermodynamics
Online Access:	Get full text
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Summary:	Mismatch is fine: Proline derivatives with a ring pucker mismatching that of natural collagen but with favorable torsional angles along the peptide chain are readily tolerated within the collagen triple helix (see picture). In contrast, a competition between intramolecular and interstrand H bonds destabilizes the collagen triple helix.
Bibliography:	Bachem istex:302C2C050F3E1F11ADEDD2CD6DF239347500DD0D This work was supported by the NCCR NANO and Bachem. H.W. is grateful to Bachem for an endowed professorship. ark:/67375/WNG-XQKNNR60-W NCCR NANO ArticleID:ANIE201008118 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1433-7851 1521-3773
DOI:	10.1002/anie.201008118