title: Protein dynamics from nuclear magnetic relaxation.
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.
authors.affiliation: École Normale Supérieure-PSL Research University, Département de Chimie, 24, rue Lhomond, 75005 Paris, France. Fabien.Ferrage@ens.fr.
authors.forename: Cyril
authors.initials: C
authors.lastname: Charlier
authors.forename: Samuel F
authors.initials: SF
authors.lastname: Cousin
authors.forename: Fabien
authors.initials: F
authors.lastname: Ferrage
mesh_terms: D006801:Humans; D009068:Movement; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011506:Proteins