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Science 14 April 2006:
Vol. 312. no. 5771, pp. 224 - 228
DOI: 10.1126/science.1124964
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Review

New Tools Provide New Insights in NMR Studies of Protein Dynamics

Anthony Mittermaier1 and Lewis E. Kay2

There is growing evidence that structural flexibility plays a central role in the function of protein molecules. Many of the experimental data come from nuclear magnetic resonance (NMR) spectroscopy, a technique that allows internal motions to be probed with exquisite time and spatial resolution. Recent methodological advancements in NMR have extended our ability to characterize protein dynamics and promise to shed new light on the mechanisms by which these molecules function. Here, we present a brief overview of some of the new methods, together with applications that illustrate the level of detail at which protein motions can now be observed.

1 Department of Chemistry, McGill University, Montreal, Quebec H3A 2K6, Canada. E-mail: anthony.mittermaier{at}mcgill.ca
2 Department of Medical Genetics, Department of Biochemistry, and Department of Chemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada. E-mail: kay{at}pound.med.utoronto.ca

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