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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...
| Autores principales: | , , |
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| Formato: | Online Artículo Texto |
| Lenguaje: | English |
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Nature Publishing Group UK
2017
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| Materias: | |
| 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 |