pH-Dependent cooperativity and existence of a dry molten globule in the folding of a miniprotein BBL-Reference-Cited by-同舟云学术

pH-Dependent cooperativity and existence of a dry molten globule in the folding of a miniprotein BBL

Published:2018 Issue:5 Volume:20 Page:3523-3530
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Yue Zhi¹²³⁴^ORCID,Shen Jana¹²³⁴^ORCID

Affiliation:

1. Department of Pharmaceutical Sciences

2. University of Maryland School of Pharmacy

3. Baltimore

4. USA

Abstract

Constant pH molecular dynamics simulations of BBL reveals negligible folding free energy barrier that is pH dependent and a sparsely populated dry molten globule state.

Funder

National Institute of General Medical Sciences

Directorate for Biological Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2018/CP/C7CP08296G

Reference67 articles.

1. From the first protein structures to our current knowledge of protein folding: delights and scepticisms

2. The Protein-Folding Problem, 50 Years On

3. Evolution, energy landscapes and the paradoxes of protein folding

4. The Protein Folding Problem

5. Microsecond folding experiments and simulations: a match is made

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