Affiliation:
1. Institut für Organische Chemie, Marie-Curie-Straße 11, Universität Frankfurt, D-60439 Frankfurt, Germany.
Abstract
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 ψ in the protein rhodniin, which is difficult to determine in solution by NMR spectroscopy.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
301 articles.
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