title: Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein.
abstract: We demonstrate that it is possible to record site-specific spin-lattice relaxation rates for the majority of (13)C sites in uniformly (13)C and (15)N labeled solid proteins as a result of the slowing down of proton-driven spin diffusion at sample spinning frequencies > or = 60 kHz, thus providing a series of new experimental probes for characterizing molecular dynamics in solid proteins.
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: Hans Jürgen
authors.initials: HJ
authors.lastname: Sass
authors.forename: Stephan
authors.initials: S
authors.lastname: Grzesiek
authors.forename: Martin
authors.initials: M
authors.lastname: Blackledge
authors.forename: Lyndon
authors.initials: L
authors.lastname: Emsley
mesh_terms: D002247:Carbon Isotopes; D004058:Diffusion; D008280:Magnetics; D008958:Models, Molecular; D053758:Nanoparticles; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D013997:Time Factors
chemical_list: D002247:Carbon Isotopes; D011506:Proteins