Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.

@article{Mayer1999InvestigationOT,
  title={Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy.},
  author={Matthias P. Mayer and Thomas Laufen and Klaus Paal and John S McCarty and Bernd Bukau},
  journal={Journal of molecular biology},
  year={1999},
  volume={289 4},
  pages={1131-44}
}
Hsp70 chaperones assist protein folding through ATP-regulated transient association with substrates. Substrate binding by Hsp70 is controlled by DnaJ co-chaperones which stimulate Hsp70 to hydrolyze ATP and, consequently, to close its substrate binding cavity allowing trapping of substrates. We analyzed the interaction of the Escherichia coli Hsp70 homologue, DnaK, with DnaJ using surface plasmon resonance (SPR) spectroscopy. Resonance signals of complex kinetic characteristics were detected… CONTINUE READING