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.
|Number of pages||5|
|Journal||Journal of Magnetic Resonance|
|State||Published - Apr 2000|
Bibliographical noteFunding Information:
The work was supported by NIH Grants GM52421 and GM52406. CWVK is the recipient of a University of Michigan Regents Fellowship. We thank Drs. C. Smith and M. A. Saper for preliminary coordinates of YopH. The W. M. Keck Foundation, NIH, NSF and Parke-Davis/Warner Lambert are gratefully acknowledged for financial support toward the 800 MHz NMR instrument.
- Homonuclear decoupling
- Protein assignment
- Protein structure
- Residual dipolar coupling
ASJC Scopus subject areas
- Nuclear and High Energy Physics
- Condensed Matter Physics