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Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins
BACKGROUND: The unfolding speed of some hyperthermophilic proteins is dramatically lower than that of their mesostable homologs. Ribonuclease HII from the hyperthermophilic archaeon Thermococcus kodakaraensis (Tk-RNase HII) is stabilized by its remarkably slow unfolding rate, whereas RNase HI from t...
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| Hlavní autoři: | , , , , , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
BioMed Central
2010
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2927913/ https://ncbi.nlm.nih.gov/pubmed/20615256 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1186/1471-2148-10-207 |
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