Protein dynamics from nuclear magnetic relaxation-Reference-Cited by-同舟云学术

Protein dynamics from nuclear magnetic relaxation

Published:2016 Issue:9 Volume:45 Page:2410-2422
ISSN:0306-0012
Container-title:Chemical Society Reviews
language:en
Short-container-title:Chem. Soc. Rev.

Author:

Charlier Cyril¹²³⁴⁵,Cousin Samuel F.¹²³⁴⁵,Ferrage Fabien¹²³⁴⁵

Affiliation:

1. École Normale Supérieure-PSL Research University

2. Département de Chimie

3. 75005 Paris

4. France

5. Sorbonne Universités

Abstract

Protein dynamics are explored by a variety of methods designed to measure nuclear magnetic relaxation rates.

Funder

European Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CS/C5CS00832H

Reference50 articles.

1. M. H. Levitt , Spin Dynamics: Basics of Nuclear Magnetic Resonance, John Wiley & Sons, Chichester, 2nd edn, 2008

2. D. Neuhaus and M. P.Williamson, The Nuclear Overhauser Effect in Structural and Conformational Analysis, John Wiley & Sons, New York, 2nd edn, 2000

3. Deuterium Spin Probes of Side-Chain Dynamics in Proteins. 1. Measurement of Five Relaxation Rates per Deuteron in 13C-Labeled and Fractionally 2H-Enriched Proteins in Solution

4. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity

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