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pH dependent conformational changes in the bacterial Hsp90 reveal a Grp94-like conformation at pH6 that is highly active for suppression of citrate synthase aggregation

The molecular chaperone Hsp90 depends upon large conformational rearrangements for its function. One driving force for these rearrangements is the intrinsic ATPase activity of Hsp90, as seen with other chaperones. However, unlike other chaperones, structural and kinetic studies have shown that the A...

पूर्ण विवरण

में बचाया:
ग्रंथसूची विवरण
मुख्य लेखकों: Krukenberg, Kristin A., Southworth, Daniel R., Street, Timothy O., Agard, David A.
स्वरूप: Artigo
भाषा:Inglês
प्रकाशित: 2009
विषय:
ऑनलाइन पहुंच:https://ncbi.nlm.nih.gov/pmc/articles/PMC2735500/
https://ncbi.nlm.nih.gov/pubmed/19427321
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.jmb.2009.04.080
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