A novel folding pathway of the villin headpiece subdomain HP35-Reference-Cited by-同舟云学术

A novel folding pathway of the villin headpiece subdomain HP35

Published:2019 Issue:33 Volume:21 Page:18219-18226
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Wang Ercheng¹²³⁴^ORCID,Tao Peng⁵⁶⁷⁸⁴^ORCID,Wang Jun⁵⁶⁷⁸⁴^ORCID,Xiao Yi⁵⁶⁷⁸⁴^ORCID

Affiliation:

1. College of Pharmaceutical Sciences

2. Zhejiang University

3. Hangzhou

4. China

5. Institute of Biophysics

6. School of Physics

7. Huazhong University of Science and Technology

8. Wuhan 430074

Abstract

Six folding states and three folding pathways are identified for HP35 with U and F being unfolded and folded states and I1, I2, I3 and I4 being intermediate states.

Funder

National Natural Science Foundation of China

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2019/CP/C9CP01703H

Reference38 articles.

1. A Thermostable 35-Residue Subdomain within Villin Headpiece

2. NMR structure of the 35-residue villin headpiece subdomain

3. High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein

4. Experimental Tests of Villin Subdomain Folding Simulations

5. Common Structural Transitions in Explicit-Solvent Simulations of Villin Headpiece Folding

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