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Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

The molecular chaperone, Hsp90, is an essential eukaryotic protein that assists in the maturation and activation of client proteins. Hsp90 function depends upon the binding and hydrolysis of ATP, which causes large conformational rearrangements in the chaperone. Hsp90 is highly conserved from bacter...

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Detaylı Bibliyografya
Asıl Yazarlar: Krukenberg, Kristin A, Böttcher, Ulrike M K, Southworth, Daniel R, Agard, David A
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Wiley Subscription Services, Inc., A Wiley Company 2009
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2777357/
https://ncbi.nlm.nih.gov/pubmed/19554567
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.191
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