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Following protein folding in real time using NMR spectroscopy

Nature Structural Biology volume 2, pages 865–870 (1995)Cite this article

Abstract

The refolding of apo bovine α-lactalbumin has been monitored in real time by NMR spectroscopy following rapid in situ dilution of a chemically denatured state. By examining individual resonances in the time-resolved NMR spectra, the native state has been shown to emerge in a cooperative manner from an intermediate formed in the dead-time of the experiments. The kinetics of folding to the native state are closely similar to those observed by stopped-flow fluorescence and near-UV circular dichroism. The NMR spectrum of the transient intermediate resembles closely that of the well characterized stable molten globule state formed at low pH. The results suggest that NMR can play a key role in describing at an atomic level the structural transitions occurring during protein folding.

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Authors and Affiliations

  1. Oxford Centre for Molecular Sciences, New Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QT, UK

    Jochen Balbach, Vincent Forge, Nico A. J. van Nuland & Christopher M. Dobson

  2. Oxford Centre for Molecular Sciences, Physical and Theoretical Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QZ, UK

    Steve L. Winder & Peter J. Hore

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  1. Jochen Balbach
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  4. Steve L. Winder
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  6. Christopher M. Dobson
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Balbach, J., Forge, V., van Nuland, N. et al. Following protein folding in real time using NMR spectroscopy. Nat Struct Mol Biol 2, 865–870 (1995). https://doi.org/10.1038/nsb1095-865

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