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...
Guardado en:
| Publicado en: | Proc Natl Acad Sci U S A |
|---|---|
| Autores principales: | , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
National Academy of Sciences
1993
|
| Materias: | |
| Acceso en línea: | 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 |
| Etiquetas: |
Sin Etiquetas, Sea el primero en etiquetar este registro!
|