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A novel conformation of E. coli Hsp90 in solution: insights into the conformational dynamics of Hsp90

Hsp90, an essential eukaryotic chaperone, depends upon its intrinsic ATPase activity for function. Crystal structures of the bacterial Hsp90 homolog, HtpG, and the yeast Hsp90 reveal large domain rearrangements between the nucleotide-free and the nucleotide-bound forms. Using small-angle x-ray scatt...

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Detalhes bibliográficos
Main Authors: Krukenberg, K.A., Förster, F., Rice, L.M., Sali, A., Agard, D.A.
Formato: Artigo
Idioma:Inglês
Publicado em: 2008
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2600884/
https://ncbi.nlm.nih.gov/pubmed/18462680
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2008.01.021
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