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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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| Vydáno v: | Sci Rep |
|---|---|
| Hlavní autoři: | , , , , , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Nature Publishing Group UK
2018
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| Témata: | |
| On-line přístup: | 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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