NMR Method for Characterizing Microsecond-to-Millisecond Chemical Exchanges Utilizing Differential Multiple-Quantum Relaxation in High Molecular Weight Proteins-Reference-Cited by-同舟云学术

NMR Method for Characterizing Microsecond-to-Millisecond Chemical Exchanges Utilizing Differential Multiple-Quantum Relaxation in High Molecular Weight Proteins

Published:2016-02-08 Issue:7 Volume:138 Page:2302-2311
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Toyama Yuki¹²,Osawa Masanori¹,Yokogawa Mariko¹,Shimada Ichio¹

Affiliation:

1. Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan

2. Japan Biological Informatics Consortium (JBIC), Aomi, Koto-ku, Tokyo 135-0064, Japan

Funder

Ministry of Education, Culture, Sports, Science, and Technology

Ministry of Economy, Trade and Industry

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.5b12954

Reference91 articles.

1. NMR spectroscopy brings invisible protein states into focus

2. Functional dynamics of proteins revealed by solution NMR

3. Nuclear Magnetic Resonance Methods for Quantifying Microsecond-to-Millisecond Motions in Biological Macromolecules

4. Fast Kinetics and Mechanisms in Protein Folding

5. Multiple Conformational Changes in Enzyme Catalysis

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