Direct Measurement of Angles Between Bond Vectors in High-Resolution NMR
Bernd Reif,
Mirko Hennig,
Christian Griesinger
*
Angles between two interatomic vectors are measured for structure
elucidation in solution nuclear magnetic resonance (NMR). The angles
can be determined directly by using the effects of dipole-dipole
cross-correlated relaxation of double-quantum and zero-quantum
coherences. The measured rates can be directly related to the angular
geometry without need for calibration of a Karplus-type curve, as is
the case for scalar coupling measurements, and depend only on the
rotational correlation time of the molecule as an empirical parameter.
This makes the determination of torsional angles independent from the
measurement of coupling constants. The two interatomic vectors can in
principle be arbitrarily far apart. The method was demonstrated on the
measurement of the peptide backbone angle
in the protein rhodniin,
which is difficult to determine in solution by NMR spectroscopy.
Institut für Organische Chemie, Marie-Curie-Straße 11, Universität Frankfurt, D-60439 Frankfurt, Germany.
*
To whom correspondence should be addressed. E-mail:
cigr{at}krypton.org.chemie.uni-frankfurt.de