The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis

@article{Mickler2009TheLC,
  title={The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis},
  author={Moritz Mickler and Martin Hessling and Christoph Ratzke and Johannes Buchner and Thorsten Hugel},
  journal={Nature Structural &Molecular Biology},
  year={2009},
  volume={16},
  pages={281-286}
}
The molecular chaperone heat-shock protein 90 (Hsp90) is one of the most abundant proteins in unstressed eukaryotic cells. Its function is dependent on an exceptionally slow ATPase reaction that involves large conformational changes. To observe these conformational changes and to understand their interplay with the ATPase function, we developed a single-molecule assay that allows examination of yeast Hsp90 dimers in real time under various nucleotide conditions. We detected conformational… CONTINUE READING
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