Nature Structural Biology
4, 801 - 804 (1997)
doi:10.1038/nsb1097-801
Structure of a kinetic protein folding intermediate by equilibrium amide exchangeLaszlo L. P. Hosszu1, C. Jeremy Craven1, Martin J. Parker2, Mark Lorch2, James Spencer2, 3, Anthony R. Clarke2, 5
& Jonathan P. Waltho1, 4
1Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield S10 2UH, U.K.
2Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol BS8 1TD, U.K.
3Present address: Division of Protein Structure, National Institute for Medical Research, The Ridgeway, London NW7 1AA, U.K.
4email:j.waltho@sheffield.ac.uk
5email:darkear@bsa.bristol.ac.uk A combination of equilibrium amide exchange and kinetic folding data show that the essential features of the complex topology of the N-terminal domain of a thermophilic phosphoglycerate kinase are established on a millisecond or faster timescale, before the rate-limiting step in the folding pathway commences.
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