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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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| Hauptverfasser: | , |
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| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
2003
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| Schlagworte: | |
| Online Zugang: | 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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