Magnetization transfer via residual dipolar couplings: application to proton-proton correlations in partially aligned proteins.
A novel three-dimensional NMR experiment is reported that allows the observation of correlations between amide and other protons via residual dipolar couplings in partially oriented proteins. The experiment is designed to permit quantitative measurement of the magnitude of proton-proton residual dipolar couplings in larger molecules and at higher degree of alignments. The observed couplings contain data valuable for protein resonance assignment, local protein structure refinement, and determination of low-resolution protein folds.
Pellecchia
M
M
Biophysics Research Division, Department of Chemistry, Department of Biological Chemistry, The University of Michigan, Ann Arbor, Michigan 48109, USA.
Vander Kooi
C W
CW
Keliikuli
K
K
Zuiderweg
E R
ER
D000465:Algorithms; D000577:Amides; D020816:Amino Acid Motifs; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011487:Protein Conformation; D017510:Protein Folding; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*; D011522:Protons; D015007:Yersinia / Q000737:chemistry
D000577:Amides; D001425:Bacterial Outer Membrane Proteins; D011522:Protons; D006859:Hydrogen; D017027:Protein Tyrosine Phosphatases; C067571:yopH protein, Yersinia