Quantifying the Intrinsic Conformation Energy Landscape Topography of Proteins with Large-Scale Open–Closed Transition-Reference-Cited by-同舟云学术

Quantifying the Intrinsic Conformation Energy Landscape Topography of Proteins with Large-Scale Open–Closed Transition

Published:2018-08-01 Issue:8 Volume:4 Page:1015-1022
ISSN:2374-7943
Container-title:ACS Central Science
language:en
Short-container-title:ACS Cent. Sci.

Author:

Chu Wen-Ting¹^ORCID,Wang Jin¹²^ORCID

Affiliation:

1. State Key Laboratory of Electroanalytical Chemistry, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, Changchun, Jilin 130022, China

2. Department of Chemistry & Physics, State University of New York at Stony Brook, Stony Brook, New York 11794, United States

Funder

Ministry of Science and Technology of the People's Republic of China

National Natural Science Foundation of China

Division of Physics

Publisher

American Chemical Society (ACS)

Subject

General Chemical Engineering,General Chemistry

Link

http://pubs.acs.org/doi/pdf/10.1021/acscentsci.8b00274

Reference56 articles.

1. Space-Filling Models of Kinase Clefts and Conformation Changes

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4. Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme

5. Linkage between dynamics and catalysis in a thermophilic-mesophilic enzyme pair

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