Collective reorientational motion and nuclear spin relaxation in proteins.
Significant progress in NMR methodology for measuring spin-relaxation data at many different 15N and 13C sites in proteins demands new and increasingly sophisticated ways of data interpretation. Recent work of our group concerning the use of anisotropic and reorientational collective motional models for spin-relaxation interpretation is briefly reviewed and a number of important aspects of collective reorientational motional models are discussed at the example of a 11 ns molecular dynamics computer simulation of the protein ubiquitin.
Carlson School of Chemistry and Biochemistry, Clark University, Worcester, MA 01610-1477, USA.
J J
JJ
Prompers
S F
SF
Lienin
R
R
Brüschweiler
D016880:Anisotropy; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D009038:Motion; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics; D014452:Ubiquitins / Q000737:chemistry
D011506:Proteins; D014452:Ubiquitins