Inactivation and Unfolding of Protein Tyrosine Phosphatase from Thermus thermophilus HB27 during Urea and Guanidine Hydrochloride Denaturation

The effects of urea and guanidine hydrochloride (GdnHCl) on the activity, conformation and unfolding process of protein tyrosine phosphatase (PTPase), a thermostable low molecular weight protein from Thermus thermophilus HB27, have been studied. Enzymatic activity assays showed both urea and GdnHCl...

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Detaylı Bibliyografya
Asıl Yazarlar: Wang, Yejing, He, Huawei, Liu, Lina, Gao, Chunyan, Xu, Shui, Zhao, Ping, Xia, Qingyou
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: Public Library of Science 2014
Konular:
Research Article
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC4177882/
https://ncbi.nlm.nih.gov/pubmed/25255086
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1371/journal.pone.0107932
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