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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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Bibliographic Details
Main Authors: Morjana, N A, McKeone, B J, Gilbert, H F
Format: Artigo
Language:Inglês
Published: 1993
Subjects:
Online Access:https://ncbi.nlm.nih.gov/pmc/articles/PMC46034/
https://ncbi.nlm.nih.gov/pubmed/8460117
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