Abstract
Recent progress has advanced our abilities to use NMR spectroscopy to follow -- in real time -- the structural and dynamic changes taking place during protein folding.
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Acknowledgements
Acknowledgments
We thank J. Balbach, V. Forge, J. A. Jones, N. A. J. van Nuland and S. L. Winder, for many of the ideas that have gone into the work from our own laboratories and that is discussed here. We are grateful to J. Baum, H. B. Gray, R. Kaptein and J. Balbach for kindly providing reprints of unpublished work, and to C. Freiden and J. Baum for copies of Figs 1 and 2. The Oxford Centre for Molecular Sciences is supported by BBSRC, EPSRC and MRC. The research of C.M.D. is also supported by the Howard Hughes Medical Institute and the Wellcome Trust.
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Dobson, C., Hore, P. Kinetic studies of protein folding using NMR spectroscopy. Nat Struct Mol Biol 5 (Suppl 7), 504–507 (1998). https://doi.org/10.1038/744
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DOI: https://doi.org/10.1038/744
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