Nanosecond Time Scale Motions in Proteins Revealed by High-Resolution NMR Relaxometry-Reference-Cited by-同舟云学术

Nanosecond Time Scale Motions in Proteins Revealed by High-Resolution NMR Relaxometry

Published:2013-11-26 Issue:49 Volume:135 Page:18665-18672
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Charlier Cyril¹,Khan Shahid Nawaz¹,Marquardsen Thorsten²,Pelupessy Philippe¹,Reiss Volker²,Sakellariou Dimitris¹³,Bodenhausen Geoffrey¹⁴,Engelke Frank²,Ferrage Fabien¹

Affiliation:

1. Laboratoire des Biomolécules, Département de Chimie, UMR 7203 CNRS-UPMC-ENS, Ecole Normale Supérieure, 24 Rue Lhomond, 75231 Paris Cedex 05, France

2. Bruker BioSpin GmbH, Silberstreifen 4, D 76287 Rheinstetten, Germany

3. Laboratoire Structure et Dynamique par Résonance Magnétique, UMR 3299-SIS2M CEA/CNRS, IRAMIS, DSM, CEA Saclay, F-91191, Gif-sur-Yvette Cedex, France

4. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, BCH, 1015 Lausanne, Switzerland

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja409820g

Reference63 articles.

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2. General Framework for Studying the Dynamics of Folded and Nonfolded Proteins by NMR Relaxation Spectroscopy and MD Simulation

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

4. Deviations from the simple two-parameter model-free approach to the interpretation of nitrogen-15 nuclear magnetic relaxation of proteins

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