title: Observation of heteronuclear overhauser effects confirms the 15N-1H dipolar relaxation mechanism in a crystalline protein.
abstract: The observation of proton to nitrogen-15 heteronuclear Overhauser effects in the microcrystalline protein Crh is used to confirm that the principal mechanism of relaxation of amide nitrogens is due to the fluctuation of the N-H dipolar couplings caused by N-H bond dynamics. Our observations reveal the central role of water as the main source of proton magnetization, and we provide an analysis of the different pathways that could lead to the observed results.
authors.affiliation: Laboratoire de Chimie (UMR 5182 CNRS/ENS), Ecole Normale Supérieure de Lyon, 69364 Lyon, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Giraud
authors.forename: Julien
authors.initials: J
authors.lastname: Sein
authors.forename: Guido
authors.initials: G
authors.lastname: Pintacuda
authors.forename: Anja
authors.initials: A
authors.lastname: Böckmann
authors.forename: Anne
authors.initials: A
authors.lastname: Lesage
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*; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010750:Phosphoproteins / Q000737:chemistry*; D011522:Protons
chemical_list: D001426:Bacterial Proteins; C118042:Crh protein, Bacillus subtilis; D009587:Nitrogen Isotopes; D010750:Phosphoproteins; D011522:Protons