title: Site-specific backbone dynamics from a crystalline protein by solid-state NMR spectroscopy.
abstract: Site-specific nitrogen-15 longitudinal relaxation rates are measured for the microcrystalline dimeric form of the protein Crh using multidimensional high-resolution solid-state NMR methods. The measured rates are used to provide a qualitative description of the site-specific internal mobility of the protein present in the solid state.
authors.affiliation: Laboratoire de Chimie, UMR 5182 CNRS/ENS, Laboratoire de Recherche Conventionné du CEA (no. 23V), Ecole Normale Supérieure de Lyon, 69364 Lyon, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Giraud
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.forename: Anne
authors.initials: A
authors.lastname: Lesage
authors.forename: François
authors.initials: F
authors.lastname: Penin
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
authors.forename: Lyndon
authors.initials: L
authors.lastname: Emsley
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003460:Crystallization; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary
chemical_list: D001426:Bacterial Proteins; D009587:Nitrogen Isotopes; D010750:Phosphoproteins