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Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry

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Abstract

The conformation of a three-disulphide derivative of bovine α-lactalbumin bound to the molecular chaperone GroEL has been investigated by monitoring directly its hydrogen exchange kinetics using electrospray ionization mass spectrometry. The bound protein is weakly protected from exchange to an extent closely similar to that of an uncomplexed molten globule state of the three-disulphide protein. Binding to GroEL in this system appears to involve relatively disordered partly folded states resembling intermediates formed in the very early stages of kinetic folding of many proteins in vitro.

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Author notes

  1. Jonathan J. Ewbank

    Present address: Department of Biology, McGill University, 1205 Docteur Penfield Avenue, Montreal, PQ, H3A 1B1, Canada

Authors and Affiliations

  1. Dyson Perrins Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford, 0X1 3QT, UK

    Carol V. Robinson

  2. New Chemistry Laboratory, Oxford Centre for Molecular Sciences, University of Oxford, South Parks Road, Oxford, 0X1 3QT, UK

    Michael Groß, Stephen J. Eyles, Christopher M. Dobson & Sheena E. Radford

  3. European Molecular Biology Laboratory, Postfach 10.2209, Meyerhofstrasse 1, 69117, Heidelberg, Germany

    Jonathan J. Ewbank

  4. Cellular Biochemistry and Biophysics Program and Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, New York, NY, 10021, USA

    Mark Mayhew & F. Ulrich Hartl

Authors
  1. Carol V. Robinson
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  2. Michael Groß
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  3. Stephen J. Eyles
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  4. Jonathan J. Ewbank
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  6. F. Ulrich Hartl
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  7. Christopher M. Dobson
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  8. Sheena E. Radford
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Robinson, C., Groß, M., Eyles, S. et al. Conformation of GroEL-bound α-lactalbumin probed by mass spectrometry. Nature 372, 646–651 (1994). https://doi.org/10.1038/372646a0

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