Molecular alignment of proteins in bicellar solutions: Quantitative evaluation of effects induced in 2D COSY spectra

Brunner, Eike and Ogle, James and Wenzler, Michael and Kalbitzer, Hans Robert (2000) Molecular alignment of proteins in bicellar solutions: Quantitative evaluation of effects induced in 2D COSY spectra. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 272 (3). pp. 694-698. ISSN 0006-291X

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Abstract

Partial molecular alignment leads to an incomplete averaging of anisotropic magnetic interactions such as magnetic dipole interaction or chemical shift anisotropy. In the present contribution we quantitatively describe and evaluate the effects induced by the addition of magnetically oriented lipid bicelles in homonuclear two-dimensional (2D) NMR correlation (COSY) spectra of proteins. It is shown that 2D COSY experiments allow the measurement of H-N-H-alpha residual dipole couplings of positive sign which can be used for structure refinement. In contrast to the double- and triple-resonance experiments previously proposed, these measurements can be carried out even on nonisotope-enriched samples. (C) 2000 Academic Press.

Item Type: Article
Uncontrolled Keywords: RESIDUAL DIPOLAR COUPLINGS; NUCLEAR MAGNETIC-RESONANCE; LIQUID-CRYSTALLINE MEDIUM; HIGH-RESOLUTION; NMR-SPECTRA; MACROMOLECULES; SPECTROSCOPY; HYDRATION; DISTANCES; RANGE;
Subjects: 500 Science > 570 Life sciences
Divisions: Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Alumni or Retired > Prof. Dr. Eike Brunner
Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Depositing User: Dr. Gernot Deinzer
Date Deposited: 05 Apr 2022 13:04
Last Modified: 05 Apr 2022 13:04
URI: https://pred.uni-regensburg.de/id/eprint/42401

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