Measurement of Site-Specific C-13 Spin-Lattice Relaxation in a Crystalline Protein
2010
Abstract
We demonstrate that it is possible to record site-specific spin-lattice relaxation rates for the majority of C-13 sites in uniformly C-13 and N-15 labeled solid proteins as a result of the slowing down of proton-driven spin diffusion at sample spinning frequencies >= 60 kHz, thus providing a series of new experimental probes for characterizing molecular dynamics in solid proteins.
Details
Title
Measurement of Site-Specific C-13 Spin-Lattice Relaxation in a Crystalline Protein
Author(s)
Lewandowski, Jozef R. ; Sein, Julien ; Sass, Hans Juergen ; Grzesiek, Stephan ; Blackledge, Martin ; Emsley, Lyndon
Published in
Journal of the American Chemical Society
Volume
132
Issue
24
Pages
8252-8254
Date
2010
Publisher
AMER CHEMICAL SOC
ISSN
0002-7863
Other identifier(s)
View record in Web of Science
Laboratories
LRM
Record Appears in
Scientific production and competences > SB - School of Basic Sciences > ISIC - Institute of Chemical Sciences and Engineering > LRM - Laboratory of Magnetic Resonance
Peer-reviewed publications
Work outside EPFL
Journal Articles
Published
Peer-reviewed publications
Work outside EPFL
Journal Articles
Published
Record creation date
2015-01-08