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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...
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| Veröffentlicht in: | Sci Rep |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artigo |
| Sprache: | Inglês |
| Veröffentlicht: |
Nature Publishing Group UK
2017
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| Schlagworte: | |
| Online Zugang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC5575259/ https://ncbi.nlm.nih.gov/pubmed/28851879 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-017-07501-4 |
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