Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in Water-Reference-Cited by-同舟云学术

Origin of β-Hairpin Stability in Solution: Structural and Thermodynamic Analysis of the Folding of a Model Peptide Supports Hydrophobic Stabilization in Water

Published:1998-02-24 Issue:9 Volume:120 Page:1996-2007
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Maynard Allister J.¹,Sharman Gary J.¹,Searle Mark S.¹

Affiliation:

1. Contribution from the Department of Chemistry, University of Nottingham, University Park, Nottingham NG7 2RD, U.K.

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja9726769

Reference73 articles.

1. The Mechanism of alpha-Helix Formation by Peptides

2. Turns in Peptides and Proteins

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

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

5. Turn Residue Sequence Determines β-Hairpin Conformation in Designed Peptides

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