Resonance Assignments of Lowly Populated and Unstable Enzyme Intermediate Complex under Real‐Time Conditions-Reference-Cited by-同舟云学术

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Resonance Assignments of Lowly Populated and Unstable Enzyme Intermediate Complex under Real‐Time Conditions

Published:2019-10 Issue:21 Volume:20 Page:2738-2742
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Chen Jia‐Liang¹,Wang Xiao¹,Xiao Yu‐Hao¹,Su Xun‐Cheng¹^ORCID

Affiliation:

1. State Key Laboratory of Elemento-Organic ChemistryCollege of ChemistryNankai University Tianjin 300071 P.R. China

Funder

National Natural Science Foundation of China

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.201900240

Reference36 articles.

1. Dynamic personalities of proteins

2. NMR paves the way for atomic level descriptions of sparsely populated, transiently formed biomolecular conformers

3. NMR Characterization of the Dynamics of Biomacromolecules

4.

5. Real-time protein NMR spectroscopy and investigation of assisted protein folding

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1. 3D Structure of the Transient Intermediate of the Enzyme–Substrate Complex of Sortase A Reveals How Calcium Binding and Substrate Recognition Cooperate in Substrate Activation;ACS Catalysis;2023-08-18

2. Highly sensitive monitoring of telomerase activity in living cells based on rapidly triggered cascade amplification reaction;Biosensors and Bioelectronics;2022-11

3. Paramagnetic Chemical Probes for Studying Biological Macromolecules;Chemical Reviews;2022-01-27

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