New approaches to the dynamic interpretation and prediction of NMR relaxation data from proteins.
NMR relaxation experiments of isotopically labeled proteins provide a wealth of information on reorientational global and local dynamics on nanosecond and subnanosecond timescales for folded and nonfolded proteins in solution. Recent methodological advances in the interpretation of relaxation data have led to a better understanding of the overall tumbling behavior, the separability of internal and overall motions, and the presence of correlated dynamics between different nuclear sites, as well as to new insights into the relationship between reorientational dynamics and primary and tertiary protein structure. Some of the new methods are particularly useful when dealing with nonfolded protein states.
Brüschweiler
Rafael
R
Carlson School of Chemistry and Biochemistry, Clark University, 950 Main Street, Worcester, MA 01610-1477, USA. bruschweiler@nmr.clarku.edu
D000465:Algorithms; D000595:Amino Acid Sequence; D003461:Crystallography / Q000379:methods*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D013113:Spin Labels; D013329:Structure-Activity Relationship
D011506:Proteins; D013113:Spin Labels