The regulation mechanism of phosphorylation and mutations in intrinsically disordered protein 4E-BP2-Reference-Cited by-同舟云学术

The regulation mechanism of phosphorylation and mutations in intrinsically disordered protein 4E-BP2

Published:2020 Issue:5 Volume:22 Page:2938-2948
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Wang Ke¹²³⁴⁵,Ning Shangbo¹²³⁴⁵,Guo Yue¹²³⁴⁵,Duan Mojie¹²³⁴⁵^ORCID,Yang Minghui¹²³⁴⁵^ORCID

Affiliation:

1. Key Laboratory of Magnetic Resonance in Biological Systems

2. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics

3. National Center for Magnetic Resonance in Wuhan

4. Wuhan Institute of Physics and Mathematics

5. Chinese Academy of Sciences

Abstract

The free energy landscapes of 4E-BP2 and its variants were obtained by replica-exchanged molecular dynamics, which elucidate the regulation mechanism of phosphorylation and mutations on the intrinsically disordered protein.

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/2020/CP/C9CP05888E

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