How DNA affects the hyperthermophilic protein Ape10b2 for oligomerization: an investigation using multiple short molecular dynamics simulations-Reference-Cited by-同舟云学术

How DNA affects the hyperthermophilic protein Ape10b2 for oligomerization: an investigation using multiple short molecular dynamics simulations

Published:2021 Issue:45 Volume:23 Page:25841-25849
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Zhang Xue¹,Zheng Qingchuan¹²^ORCID

Affiliation:

1. Institute of Theoretical Chemistry, College of Chemistry, Jilin University, Changchun, 130023, People's Republic of China

2. Key Laboratory for Molecular Enzymology and Engineering of the Ministry of Education, Jilin University, Changchun, 130023, People's Republic of China

Abstract

Ape10b2 can stabilize DNA at high temperature and DNA disturbance of the protein is beneficial for oligomerization.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2021/CP/D1CP04341B

Reference48 articles.

1. DNA bending: the prevalence of kinkiness and the virtues of normality

2. Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes

3. An Abundant DNA Binding Protein from the Hyperthermophilic Archaeon Sulfolobus shibatae Affects DNA Supercoiling in a Temperature-Dependent Fashion

4. Electron microscopic study of DNA complexes with proteins from the Archaebacterium Sulfolobus acidocaldarius

5. Crystal structure of an archaeal specific DNA-binding protein (Ape10b2) fromAeropyrum pernixK1

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