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## 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 admixed 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. © 2001 John Wiley & Sons, Inc. Concepts Magn Reson 13: 238–259, 20

Who reads Residual dipolar couplings in protein NMR?

Author

Eike Brunner

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 1043-7347)

Published

2001

Language

EN

Field

Chemistry (Physical Sciences)