Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides-Reference-Cited by-同舟云学术

Assessing backbone solvation effects in the conformational propensities of amino acid residues in unfolded peptides

Published:2015 Issue:38 Volume:17 Page:24917-24924
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Ilawe Niranjan V.¹²³⁴⁵,Raeber Alexandra E.¹²³⁴⁵,Schweitzer-Stenner Reinhard⁶⁷⁸⁵,Toal Siobhan E.⁶⁷⁸⁵,Wong Bryan M.¹²³⁴⁵^ORCID

Affiliation:

1. Department of Chemical & Environmental Engineering

2. and Materials Science & Engineering Program

3. University of California

4. Riverside

5. USA

6. Department of Chemistry

7. Drexel University

8. Philadelphia

Abstract

Large energetic contributions to the stabilization of polyproline II result from peptide–water, water–water interactions, and changes of the solvent self-energy.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2015/CP/C5CP03646A

Reference59 articles.

1. The Configuration of Random Polypeptide Chains. II. Theory

2. P. J. Flory , Statistical Mechanics of Chain Molecules, Wiley & Sons, New York, 1969

3. Stereochemistry of polypeptide chain configurations

4. Protein Denaturation

5. Polyproline II propensities from GGXGG peptides reveal an anticorrelation with -sheet scales

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