Characterizing semilocal motions in proteins by NMR relaxation studies.
The understanding of protein function is incomplete without the study of protein dynamics. NMR spectroscopy is valuable for probing nanosecond and picosecond dynamics via relaxation studies. The use of 15N relaxation to study backbone dynamics has become virtually standard. Here, we propose to measure the relaxation of additional nuclei on each peptide plane allowing for the observation of anisotropic local motions. This allows the nature of local motions to be characterized in proteins. As an example, semilocal rotational motion was detected for part of a helix of the protein Escherichia coli flavodoxin.
Fischer
M W
MW
Biophysics Research Division, The University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109, USA.
Zeng
L
L
Majumdar
A
A
Zuiderweg
E R
ER
D004926:Escherichia coli; D005418:Flavodoxin / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D011487:Protein Conformation
D005418:Flavodoxin