Structural and Functional Analysis of the Middle Segment of Hsp 90 : Implications for ATP Hydrolysis and Client

@inproceedings{Meyer2003StructuralAF,
  title={Structural and Functional Analysis of the Middle Segment of Hsp 90 : Implications for ATP Hydrolysis and Client},
  author={Philippe Meyer and Chrisostomos Prodromou and Bin Hu and Cara K. Vaughan and S. Mark Roe and Barry Panaretou and Peter W Piper and Laurence H. Pearl},
  year={2003}
}
standing the mechanistic biochemistry of Hsp90 itself, little is known about how the ATPase-coupled confor-mational chaperone cycle promotes client protein activation , or even where and how Hsp90 interacts with its disparate, but nonetheless specific, clients.; however , these utilized peptides and denatured proteins not 2 Division of Life Sciences King's College London known to be Hsp90 clients in vivo. Furthermore, Hsp90 in vivo is not involved in binding of denatured proteins Franklin… CONTINUE READING