Protein dynamics from nuclear magnetic relaxation. (2nd March 2016)

• Record Type: Journal Article
• Authors: Charlier, Cyril; Cousin, Samuel F.; Ferrage, Fabien
• Is Part Of: Chemical Society reviews. Volume 45:Number 9(2016:May)
• Page Start: 2410
• Page End: 2422
• Publication Date: 2016-03-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c5cs00832h
• Languages: English
• ISSNs: 0306-0012

Abstract

Abstract : Protein dynamics are explored by a variety of methods designed to measure nuclear magnetic relaxation rates. Abstract : Nuclear magnetic resonance is a ubiquitous spectroscopic tool to explore molecules with atomic resolution. Nuclear magnetic relaxation is intimately connected to molecular motions. Many methods and models have been developed to measure and interpret the characteristic rates of nuclear magnetic relaxation in proteins. These approaches shed light on a rich and diverse range of motions covering timescales from picoseconds to seconds. Here, we introduce some of the basic concepts upon which these approaches are built and provide a series of illustrations.