Refolding kinetics of cytochrome c(551) reveals a mechanistic difference between urea and guanidine

The energetic parameters for the folding of small globular proteins can be very different if derived from guanidine hydrochloride (GdnHCl) or urea denaturation experiments. A study of the equilibrium and kinetics of the refolding of wild-type (wt) cytochrome c(551) (cyt c(551)) from Pseudomonas aeru...

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Detaylı Bibliyografya
Asıl Yazarlar: Gianni, Stefano, Brunori, Maurizio, Travaglini-Allocatelli, Carlo
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Cold Spring Harbor Laboratory Press 2001
Konular:
For the Record
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2374076/
https://ncbi.nlm.nih.gov/pubmed/11468365
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