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Interdomain communication in the molecular chaperone DnaK.

DnaK, a heat-shock protein 70 (Hsp70) homologue in Escherichia coli, possesses a single tryptophan residue in its ATPase domain. Changes in the intrinsic fluorescence of DnaK offer a simple means not only to follow the binding of ATP and of ADP plus the co-chaperone GrpE to the ATPase domain, but al...

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Bibliografische gegevens
Hoofdauteurs: Han, Wanjiang, Christen, Philipp
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: 2003
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC1223109/
https://ncbi.nlm.nih.gov/pubmed/12383055
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20020943
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