title: Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteins.
abstract: A model for calculating the influence of anisotropic collective motions on NMR relaxation rates in crystalline proteins is presented. We show that small-amplitude (<10 degrees ) fluctuations may lead to substantial contributions to the (15)N spin-lattice relaxation rates and propose that the effect of domain motions should be included in solid-state NMR analyses of protein dynamics.
authors.affiliation: Université de Lyon, CNRS/ENS-Lyon/UCB-Lyon 1, Centre de RMN à Très Hauts Champs, 69100 Villeurbanne, France.
authors.forename: Józef R
authors.initials: JR
authors.lastname: Lewandowski
authors.forename: Julien
authors.initials: J
authors.lastname: Sein
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
authors.forename: Lyndon
authors.initials: L
authors.lastname: Emsley
mesh_terms: D016880:Anisotropy; D003460:Crystallization; D008958:Models, Molecular; D009038:Motion; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins