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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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1993
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC46034/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/8460117/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.90.6.2107 |
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