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 resul
ting so-called "residual" anisotropic magnetic interactions currently becom
e increasingly important in biomolecular NMR spectroscopy in particular, re
sidual dipolar couplings turn out to be extremely useful novel parameters f
or protein structure determination The basic principles of this new methodo
logy are discussed in the present review and recent applications are demons
trated. Different alignment mechanisms leading to partial orientation of pr
otein molecules in solution are considered in detail. The influence of magn
etic and electric fields applied to isotropic protein solutions is discusse
d. Various magnetically orienting media which can be admired to protein sol
utions are described and compared. Experiments for the measurement of resid
ual dipolar couplings in proteins and advantageous strategies for the use o
f residual dipolar couplings in structure calculations are reviewed. (C) 20
01 John Wiley & Sons. Inc.