Accessibility explains preferred thiol-disulfide isomerization in a protein domain

Disulfide bonds are key stabilizing and yet potentially labile cross-links in proteins. While spontaneous disulfide rearrangement through thiol-disulfide exchange is increasingly recognized to play an important physiological role, its molecular determinants are still largely unknown. Here, we used a...

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Detalles Bibliográficos
Autores principales: Kolšek, Katra, Aponte-Santamaría, Camilo, Gräter, Frauke
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5575259/
https://www.ncbi.nlm.nih.gov/pubmed/28851879
http://dx.doi.org/10.1038/s41598-017-07501-4

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5575259/
https://www.ncbi.nlm.nih.gov/pubmed/28851879
http://dx.doi.org/10.1038/s41598-017-07501-4

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