title: Protein dynamics by ¹⁵N nuclear magnetic relaxation.
abstract: Nitrogen-15 relaxation is the most ubiquitous source of information about protein (backbone) dynamics used by NMR spectroscopists. It provides the general characteristics of hydrodynamics as well as internal motions on subnanosecond, micro- and millisecond timescales of a biomolecule. Here, we present a full protocol to perform and analyze a series of experiments to measure the (15)N longitudinal relaxation rate, the (15)N transverse relaxation rate under an echo train or a single echo, the (15)N-(1)H dipolar cross-relaxation rate, as well as the longitudinal and transverse cross-relaxation rates due to the cross-correlation of the nitrogen-15 chemical shift anisotropy and the dipolar coupling with the adjacent proton. These rates can be employed to carry out model-free analyses and can be used to quantify accurately the contribution of chemical exchange to transverse relaxation.
authors.affiliation: Département de chimie, Ecole normale supérieure et Laboratoire des Biomolécules, CNRS UMR 7203, Paris, Cedex, France. Fabien.Ferrage@ens.fr
authors.forename: Fabien
authors.initials: F
authors.lastname: Ferrage
mesh_terms: D016880:Anisotropy; D006859:Hydrogen; D008956:Models, Chemical; D009587:Nitrogen Isotopes / Q000378:metabolism*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D009587:Nitrogen Isotopes; D011506:Proteins; D006859:Hydrogen