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Structure of a kinetic protein folding intermediate by equilibrium amide exchange

Nature Structural Biology volume 4, pages 801–804 (1997)Cite this article

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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Author notes

  1. James Spencer

    Present address: Division of Protein Structure, National Institute for Medical Research, The Ridgeway, London, NW7 1AA, U.K.

Authors and Affiliations

  1. Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, University of Sheffield, P.O. Box 594, Sheffield, S10 2UH, U.K.

    Laszlo L. P. Hosszu, C. Jeremy Craven & Jonathan P. Waltho

  2. Department of Biochemistry, University of Bristol, School of Medical Sciences, University Walk, Bristol, BS8 1TD, U.K.

    Martin J. Parker, Mark Lorch, James Spencer & Anthony R. Clarke

Authors
  1. Laszlo L. P. Hosszu
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  2. C. Jeremy Craven
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  3. Martin J. Parker
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  4. Mark Lorch
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  5. James Spencer
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  6. Anthony R. Clarke
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  7. Jonathan P. Waltho
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Hosszu, L., Craven, C., Parker, M. et al. Structure of a kinetic protein folding intermediate by equilibrium amide exchange. Nat Struct Mol Biol 4, 801–804 (1997). https://doi.org/10.1038/nsb1097-801

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