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The cold denaturation of IscU highlights structure–function dualism in marginally stable proteins
Proteins undergo both cold and heat denaturation, but often cold denaturation cannot be detected because it occurs at temperatures below water freezing. Proteins undergoing detectable cold as well as heat denaturation yield a reliable curve of protein stability. Here we use bacterial IscU, an essent...
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| Gepubliceerd in: | Commun Chem |
|---|---|
| Hoofdauteurs: | , , , |
| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2018
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC7612454/ https://ncbi.nlm.nih.gov/pubmed/35243006 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/s42004-018-0015-1 |
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