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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Detalles Bibliográficos
Autores principales: Okada, Jun, Okamoto, Tomohiro, Mukaiyama, Atsushi, Tadokoro, Takashi, You, Dong-Ju, Chon, Hyongi, Koga, Yuichi, Takano, Kazufumi, Kanaya, Shigenori
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2927913/
https://www.ncbi.nlm.nih.gov/pubmed/20615256
http://dx.doi.org/10.1186/1471-2148-10-207

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2927913/
https://www.ncbi.nlm.nih.gov/pubmed/20615256
http://dx.doi.org/10.1186/1471-2148-10-207

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