Residual dipolar couplings in protein NMR

Brunner, Eike (2001) Residual dipolar couplings in protein NMR. CONCEPTS IN MAGNETIC RESONANCE, 13 (4). pp. 238-259. ISSN 1043-7347

Full text not available from this repository.

Abstract

Partial molecular alignment leads to an incomplete averaging of anisotropic magnetic interactions such as the magnetic dipole-dipole interaction, the chemical shift anisotropy. or the electric quadrupole interaction The resulting so-called "residual" anisotropic magnetic interactions currently become increasingly important in biomolecular NMR spectroscopy in particular, residual dipolar couplings turn out to be extremely useful novel parameters for protein structure determination The basic principles of this new methodology are discussed in the present review and recent applications are demonstrated. Different alignment mechanisms leading to partial orientation of protein molecules in solution are considered in detail. The influence of magnetic and electric fields applied to isotropic protein solutions is discussed. Various magnetically orienting media which can be admired to protein solutions are described and compared. Experiments for the measurement of residual dipolar couplings in proteins and advantageous strategies for the use of residual dipolar couplings in structure calculations are reviewed. (C) 2001 John Wiley & Sons. Inc.

Item Type: Article
Uncontrolled Keywords: NUCLEAR-MAGNETIC-RESONANCE; LIQUID-CRYSTALLINE MEDIUM; TOBACCO-MOSAIC-VIRUS; CROSS-CORRELATED RELAXATION; NEMATIC PHASE-TRANSITION; AC ELECTRIC-FIELDS; CHEMICAL-SHIFTS; BIOLOGICAL MACROMOLECULES; ORIENTED MACROMOLECULES; MOLECULAR ALIGNMENT; residual dipolar couplings; proteins; magnetic-field alignment; electric-field alignment; bicelles; viruses; protein structure calculation
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: Petra Gürster
Date Deposited: 06 May 2021 08:43
Last Modified: 06 May 2021 08:43
URI: https://pred.uni-regensburg.de/id/eprint/41844

Actions (login required)

View Item View Item