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Science 7 November 1997:
Vol. 278. no. 5340, p. 989
DOI: 10.1126/science.278.5340.989c
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This Week in Science

The direct measurement of bond distances and angles in macromolecules by nuclear magnetic resonance (NMR) is reported by Tjandra and Bax (p. 1111; see the news story by Service, p. 1015). They dissolved macromolecules in dilute aqueous solutions containing discotic nematic liquid crystals and magnetic particles. When the magnetic field was applied, the liquid crystalline media tended to align the macromolecule (in this case, the protein ubiquitin) so that dipolar couplings between nuclei, instead of canceling to zero, could be measured. The structure obtained is in excellent agreement with the known x-ray structure of ubiquitin, and the method should extend the size range of molecules that can be studied by solution NMR.

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Science. ISSN 0036-8075 (print), 1095-9203 (online)