Nuclear Magnetic Resonance Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Time Scales-Reference-Cited by-同舟云学术

Nuclear Magnetic Resonance Provides a Quantitative Description of Protein Conformational Flexibility on Physiologically Important Time Scales

Published:2011-03-21 Issue:14 Volume:50 Page:2735-2747
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Salmon Loïc¹,Bouvignies Guillaume²,Markwick Phineus³,Blackledge Martin¹

Affiliation:

1. Protein Dynamics and Flexibility, Institut de Biologie Structurale Jean-Pierre Ebel, CEA, CNRS, UJF UMR 5075, 41 Rue Jules Horowitz, Grenoble 38027, France

2. Departments of Molecular Genetics, Biochemistry, and Chemistry, The University of Toronto, Toronto, Ontario, Canada M5S 1A8

3. Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, Urey Hall, La Jolla, California 92003-0365, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi200177v

Reference96 articles.

1. A structural perspective on protein–protein interactions

2. The Impact of Structural Genomics: Expectations and Outcomes

3. Large conformational changes in proteins: signaling and other functions

4. The Energy Landscapes and Motions of Proteins

5. Recognition Dynamics Up to Microseconds Revealed from an RDC-Derived Ubiquitin Ensemble in Solution

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