Direct NMR observation of a substrate protein bound to the chaperonin GroEL.

@article{Horst2005DirectNO,
  title={Direct NMR observation of a substrate protein bound to the chaperonin GroEL.},
  author={R. Kenneth Horst and Eric B. Bertelsen and Jocelyne Fiaux and Gerhard Wider and Arthur L Horwich and Kurt W{\"u}thrich},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 36},
  pages={12748-53}
}
The reaction cycle and the major structural states of the molecular chaperone GroEL and its cochaperone, GroES, are well characterized. In contrast, very little is known about the nonnative states of the substrate polypeptide acted on by the chaperonin machinery. In this study, we investigated the substrate protein human dihydrofolate reductase (hDHFR) while bound to GroEL or to a single-ring analog, SR1, by NMR spectroscopy in solution under conditions where hDHFR was efficiently recovered as… CONTINUE READING
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Molecular Cloning: A Laboratory Manual (Cold

  • J. Sambrook, E. F. Fritsch, T. Maniatis
  • 1989

Dynamic NMR Spectroscopy (Academic, London)

  • J. Sandström
  • 1982

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