Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy-Reference-Cited by-同舟云学术

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Role of different β-turns in β-hairpin conformation and stability studied by optical spectroscopy

Published:2011-10-12 Issue:1 Volume:80 Page:44-60
ISSN:0887-3585
Container-title:Proteins: Structure, Function, and Bioinformatics
language:en
Short-container-title:Proteins

Author:

Wu Ling,McElheny Dan,Setnicka Vladimír,Hilario Jovencio,Keiderling Timothy A.

Funder

National Science Foundation

Publisher

Wiley

Subject

Molecular Biology,Biochemistry,Structural Biology

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/prot.23140/fullpdf

Reference79 articles.

1. Protein folding: General physical model;Ptitsyn;FEBS Lett,1981

2. Native-like β-hairpin structure in an isolated fragment from ferredoxin: NMR and CD studies of solvent effects on the N-terminal 20 residues;Searle;Protein Eng,1996

3. A short linear peptide derived from the N-terminal sequence of ubiquitin folds into a water-stable non-native β-hairpin;Searle;Nat Struct Biol,1995

4. Origin of β-hairpin stability in solution: structural and thermodynamic analysis of the folding of model peptide supports hydrophobic stabilization in water;Maynard;J Am Chem Soc,1998

5. Effect of preformed correct tertiary interactions on rapid two-state tendamistat folding - Evidence for hairpins as initiation sites for β-sheet formation;Schonbrunner;Biochemistry,1997

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