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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...

詳細記述

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書誌詳細
主要な著者: Krukenberg, Kristin A., Southworth, Daniel R., Street, Timothy O., Agard, David A.
フォーマット: Artigo
言語:Inglês
出版事項: 2009
主題:
オンライン・アクセス: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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