The second step of ATP binding to DnaK induces peptide release.

@article{Theyssen1996TheSS,
  title={The second step of ATP binding to DnaK induces peptide release.},
  author={H Theyssen and H. P. Schuster and Lars Packschies and Bernd Bukau and Jochen Reinstein},
  journal={Journal of molecular biology},
  year={1996},
  volume={263 5},
  pages={657-70}
}
The interaction of the nucleotide-free molecular chaperone DnaK (Hsp70) from Escherichia coli with nucleotides was studied under equilibrium and transient kinetic conditions. These studies used the intrinsic fluorescence signal of the single tryptophan residue (Trp102) of DnaK, or of novel fluorescent nucleotide analogs of ADP and ATP, N8-(4-N'-methylanthraniloylaminobutyl)-8-aminoadenosine 5'-di- or triphosphate (MABA-ADP and MABA-ATP) as spectroscopic probes. Titration of MABA-ADP with DnaK… CONTINUE READING

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