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The extreme hyper-reactivity of Cys94 in lysozyme avoids its amorphous aggregation
Many proteins provided with disulfide bridges in the native state undergo amorphous irreversible aggregation when these bonds are not formed. Here we show that egg lysozyme displays a clever strategy to prevent this deleterious aggregation during the nascent phase when disulfides are still absent. I...
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| Pubblicato in: | Sci Rep |
|---|---|
| Autori principali: | , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
Nature Publishing Group UK
2018
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.gov/pmc/articles/PMC6207692/ https://ncbi.nlm.nih.gov/pubmed/30375487 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s41598-018-34439-y |
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