| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10802522 | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research | 2012 | 12 Pages |
Abstract
⺠Hsp90 is a challenging molecule for NMR spectroscopy due to its big size and dynamic properties. ⺠Hsp90 domains are suitable for highâresolution NMR studies. ⺠Fullâlength Hsp90 is accessible for NMR studies using methylâspecific labelling. ⺠NMR allows mapping of interaction sites of coâchaperones and client proteins. ⺠NMR studies on the Hsp90-p53 interaction suggest various and to some extent controversial models.
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Authors
Tatiana Didenko, Afonso M.S. Duarte, G. Elif Karagöz, Stefan G.D. Rüdiger,