Enzyme–Substrate–Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry-Reference-Cited by-同舟云学术

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Enzyme–Substrate–Cofactor Dynamical Networks Revealed by High-Resolution Field Cycling Relaxometry

Published:2020-06-01 Issue:25 Volume:59 Page:2359-2370
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Rosenberg Masha M.¹,Yao Tianjiong¹,Patton Gregory C.¹,Redfield Alfred G.²,Roberts Mary F.³,Hedstrom Lizbeth¹⁴^ORCID

Affiliation:

1. Department of Biology, Brandeis University, MS009, 415 South St., Waltham, Massachusetts 02453-9110, United States

2. Department of Biochemistry, Brandeis University, MS009, 415 South Street, Waltham, Massachusetts 02453-9110, United States

3. Department of Chemistry, Boston College, 140 Commonwealth Avenue, Chestnut Hill, Massachusetts 02467-9110, United States

4. Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02453-3808, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00212

Reference28 articles.

1. An NMR Perspective on Enzyme Dynamics

2. Direct 13C-detection for carbonyl relaxation studies of protein dynamics

3. Enzyme dynamics point to stepwise conformational selection in catalysis

4. Dynamically Achieved Active Site Precision in Enzyme Catalysis

5. Molecular Dynamics Explorations of Active Site Structure in Designed and Evolved Enzymes

Cited by 2 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. Biomolecular interactions studied by low-field NMR using SABRE hyperpolarization;Chemical Science;2023

2. High Resolution 31P Field Cycling NMR Reveals Unsuspected Features of Enzyme-Substrate-Cofactor Dynamics;Frontiers in Molecular Biosciences;2022-03-31

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