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Statistical allosteric coupling to the active site indole ring flip equilibria in the FK506-binding domain
In solution, the Trp 59 indole ring at the base of the active site cleft in the FKBP domain protein FKBP12 is rotated by ~90° at a population level of 20%, relative to its canonical crystallographic orientation. NMR measurements on the homologous FK1 domains of human FKBP51 and FKBP52 indicate no ob...
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| Vydáno v: | Biophys Chem |
|---|---|
| Hlavní autoři: | , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
2014
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4476035/ https://ncbi.nlm.nih.gov/pubmed/25016286 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.bpc.2014.06.004 |
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