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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Bibliografiske detaljer
Main Authors: Okada, Jun, Okamoto, Tomohiro, Mukaiyama, Atsushi, Tadokoro, Takashi, You, Dong-Ju, Chon, Hyongi, Koga, Yuichi, Takano, Kazufumi, Kanaya, Shigenori
Format: Artigo
Sprog:Inglês
Udgivet: BioMed Central 2010
Fag:
Research Article
Online adgang: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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