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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...

पूर्ण विवरण

में बचाया:
ग्रंथसूची विवरण
मुख्य लेखकों: Okada, Jun, Okamoto, Tomohiro, Mukaiyama, Atsushi, Tadokoro, Takashi, You, Dong-Ju, Chon, Hyongi, Koga, Yuichi, Takano, Kazufumi, Kanaya, Shigenori
स्वरूप: Artigo
भाषा:Inglês
प्रकाशित: BioMed Central 2010
विषय:
ऑनलाइन पहुंच: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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