Protein structure determination in solution by NMR spectroscopy.
By Kurt Wüthrich. 1990
The introduction of nuclear magnetic resonance (NMR) spectroscopy as a second method for protein structure determination at atomic resolution, in addition to x-ray diffraction in single crystals, has already led to a significant increase in the number of known protein structures. The NMR method provides data that are in many ways complementary to those obtained from x-ray crystallography and thus promises to widen our view of protein molecules, giving a clearer insight into the relation between structure and function.
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Citations in the corpus
- An efficient algorithm for multistate protein design based on FASTER (2009, background): “targets for protein design because typical structure determination methods give an ensemble rather than a single set of coordinates.(16) To the extent that the structural diversity of an NMR ensemble reflects realistic conformational flexibility, it will be interesting to investigate the effects of ”