Scrutiny of electrostatic-driven conformational ordering of polypeptide chains in DMSO: a study with a model oligopeptide-Reference-Cited by-同舟云学术

Scrutiny of electrostatic-driven conformational ordering of polypeptide chains in DMSO: a study with a model oligopeptide

Published:2017 Issue:45 Volume:7 Page:27981-27991
ISSN:2046-2069
Container-title:RSC Advances
language:en
Short-container-title:RSC Adv.

Author:

Srivastava Kinshuk Raj¹²³⁴^ORCID,Goyal Bhupesh¹²³⁴^ORCID,Kumar Anil¹²³⁴,Durani Susheel¹²³⁴

Affiliation:

1. Department of Chemistry

2. Indian Institute of Technology Bombay

3. Mumbai-400076

4. India

Abstract

The molecular mechanism of DMSO-induced stabilisation of β-sheets is attributed to the combination of polar electrostatic interactions among side chains, and backbone desolvation through bulky side chains which promotes backbone hydrogen bonding.

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/RA/C7RA02137B

Reference96 articles.

1. Principles that Govern the Folding of Protein Chains

2. A new perspective on unfolded proteins

3. In Search of the Energetic Role of Peptide Hydrogen Bonds

4. Energetics of Protein Folding

5. Protein folding: a problem with multiple solutions

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