Role of Repeated Conformational Transitions in Substrate Binding of Adenylate Kinase-Reference-Cited by-同舟云学术

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Role of Repeated Conformational Transitions in Substrate Binding of Adenylate Kinase

Published:2022-10-12 Issue:41 Volume:126 Page:8188-8201
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Lu Jiajun¹²,Scheerer David³,Haran Gilad³^ORCID,Li Wenfei¹²^ORCID,Wang Wei¹^ORCID

Affiliation:

1. Department of Physics, National Laboratory of Solid State Microstructure, Nanjing University, Nanjing210093, China

2. Wenzhou Key Laboratory of Biophysics, Wenzhou Institute, University of Chinese Academy of Sciences, Wenzhou, Zhejiang325000, China

3. Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot761001, Israel

Funder

Israel Science Foundation

Deutsche Forschungsgemeinschaft

National Natural Science Foundation of China

H2020 European Research Council

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.2c05497

Reference66 articles.

1. Induced-fit movements in adenylate kinases

2. NMR Identification of Transient Complexes Critical to Adenylate Kinase Catalysis

3. Illuminating the mechanistic roles of enzyme conformational dynamics

4. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

Cited by 13 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Enzyme activation by urea reveals the interplay between conformational dynamics and substrate binding: a single-molecule FRET study;2024-09-01

2. Magnesium induced structural reorganization in the active site of adenylate kinase;Science Advances;2024-08-09

3. NMR and Single-Molecule FRET Insights into Fast Protein Motions and Their Relation to Function;Annual Review of Biophysics;2024-07-16

4. Elucidating Dynamics of Adenylate Kinase from Enzyme Opening to Ligand Release;Journal of Chemical Information and Modeling;2023-12-20

5. Effect of chaperone–client interaction strength on Hsp70-mediated protein folding;Chinese Physics B;2023-11-01

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