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Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins
Authors:Jun Okada  Tomohiro Okamoto  Atsushi Mukaiyama  Takashi Tadokoro  Dong-Ju You  Hyongi Chon  Yuichi Koga  Kazufumi Takano  Shigenori Kanaya
Affiliation:(1) Department of Material and Life Science, Osaka University, 2-1 Yamadaoka, 565-0871 Suita, Osaka, Japan;(2) CREST, JST, 2-1 Yamadaoka, 565-0871 Suita, Osaka, Japan
Abstract:

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 the thermophilic bacterium Thermus thermophilus (Tt-RNase HI) unfolds rapidly, comparable with to that of RNase HI from Escherichia coli (Ec-RNase HI).
Keywords:
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