The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design-Reference-Cited by-同舟云学术

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The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein design

Published:2016-06-09 Issue:7 Volume:29 Page:271-280
ISSN:1741-0126
Container-title:Protein Engineering Design and Selection
language:en
Short-container-title:Protein Engineering, Design and Selection

Author:

Childers Matthew Carter,Towse Clare-Louise,Daggett Valerie

Funder

National Institutes of Health

Publisher

Oxford University Press (OUP)

Subject

Molecular Biology,Biochemistry,Bioengineering,Biotechnology

Link

http://academic.oup.com/peds/article-pdf/29/7/271/17495596/gzw023.pdf

Reference68 articles.

1. Thermal induced unfolding of human serum albumin isomers: Assigning residual α helices to domain II

2. Toward solving the folding pathway of barnase: the complete backbone 13C, 15N, and 1H NMR assignments of its pH-denatured state.

3. A Comparison of the pH, Urea, and Temperature-denatured States of Barnase by Heteronuclear NMR: Implications for the Initiation of Protein Folding

4. Intrinsic backbone preferences are fully present in blocked amino acids

5. Cutoff Size Need Not Strongly Influence Molecular Dynamics Results for Solvated Polypeptides

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