Moeglich, Andreas and Wenzler, Michael and Kramer, Frank and Glaser, Steffen J. and Brunner, Eike (2002) Determination of residual dipolar couplings in homonuclear MOCCA-SIAM experiments. JOURNAL OF BIOMOLECULAR NMR, 23 (3). pp. 211-219. ISSN 0925-2738
Full text not available from this repository. (Request a copy)Abstract
In solutions with partial molecular alignment, anisotropic magnetic interactions such as the chemical shift anisotropy, the electric quadrupole interaction, and the magnetic dipole-dipole interaction are no longer averaged out to zero in contrast to isotropic solutions. The resulting residual anisotropic magnetic interactions are increasingly used in biological NMR studies for the determination of 3D structures of proteins and other biomolecules. In the present paper we propose a new approach allowing the measurement of residual H-N-H-alpha dipolar couplings of non-isotope enriched proteins based on the application of the MOCCA-SIAM experiment. This experiment allows the measurement of homonuclear coupling constants with an accuracy of ca. +/-0.2 Hz and is therefore particularly well suited to determine residual dipolar couplings at relatively low degrees of molecular orientation. The agreement between experimentally determined residual H-N-H-alpha couplings and calculated values is demonstrated for BPTI.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | 2D COSY SPECTRA; ACCURATE MEASUREMENT; PROTEIN-STRUCTURE; NMR; CONSTANTS; MACROMOLECULES; SPECTROSCOPY; FOLDS; ALIGNMENT; SEQUENCES; MOCCA mixing sequence; NMR; protein structure; residual dipolar couplings; SIAM experiment |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 18 Oct 2021 11:55 |
| Last Modified: | 18 Oct 2021 11:55 |
| URI: | https://pred.uni-regensburg.de/id/eprint/40117 |
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