Disulfide Bonds versus Trp⋅⋅⋅Trp Pairs in Irregular β-Hairpins: NMR Structure of Vammin Loop 3-Derived Peptides as a Case Study-Reference-Cited by-同舟云学术

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Disulfide Bonds versus Trp⋅⋅⋅Trp Pairs in Irregular β-Hairpins: NMR Structure of Vammin Loop 3-Derived Peptides as a Case Study

Published:2009-03-23 Issue:5 Volume:10 Page:902-910
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Mirassou Yasmina,Santiveri Clara M.,Pérez de Vega M. Jesús,González-Muñiz Rosario,Jiménez M. Angeles

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference74 articles.

1. NMR evidence of a short linear peptide that folds into a .beta.-hairpin in aqueous solution

2. A short linear peptide that folds into a native stable β-hairpin in aqueous solution

3. "Mirror image" reverse turns promote .beta.-hairpin formation

4. Interactions Responsible for the pH Dependence of the beta-Hairpin Conformational Population Formed by a Designed Linear Peptide

5. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin

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