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Guanidine hydrochloride stabilization of a partially unfolded intermediate during the reversible denaturation of protein disulfide isomerase.

The reversible denaturation of protein disulfide isomerase proceeds through intermediates that are stabilized by interaction with guanidine hydrochloride. At pH 7.5, the equilibrium denaturation by urea is completely reversible and the transition can be reasonably well-described by a two-state model...

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Main Authors: Morjana, N A, McKeone, B J, Gilbert, H F
格式: Artigo
語言:Inglês
出版: 1993
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在線閱讀:https://ncbi.nlm.nih.gov/pmc/articles/PMC46034/
https://ncbi.nlm.nih.gov/pubmed/8460117
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