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J. Biol. Chem., Vol. 265, Issue 36, 22059-22062, 12, 1990
K Wuthrich
Institut fur Molekularbiologie und Biophysik, Eidgenossische Technische Hochschule-Honggerberg, Zurich, Switzerland.
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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