Measurement of site-specific 13C spin-lattice relaxation in a crystalline protein.
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.
Lewandowski
Józef R
JR
Université de Lyon, CNRS/ENS-Lyon/UCB-Lyon 1, Centre de RMN à Très Hauts Champs, 69100 Villeurbanne, France.
Sein
Julien
J
Sass
Hans Jürgen
HJ
Grzesiek
Stephan
S
Blackledge
Martin
M
Emsley
Lyndon
L
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
D002247:Carbon Isotopes; D011506:Proteins