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Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues
Although the thermodynamics of protein denaturation at temperatures over 100 °C is essential for the rational design of highly stable proteins, it is not understood well because of the associated technical difficulties. We designed certain hydrophobic mutant proteins of CutA1 from Escherichia coli,...
Shranjeno v:
| izdano v: | Sci Rep |
|---|---|
| Main Authors: | , , , , , , , |
| Format: | Artigo |
| Jezik: | Inglês |
| Izdano: |
Nature Publishing Group
2015
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| Teme: | |
| Online dostop: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4620440/ https://ncbi.nlm.nih.gov/pubmed/26497062 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/srep15545 |
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