Evolution and thermodynamics of the slow unfolding of hyperstable monomeric proteins |
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| Authors: | Jun Okada Tomohiro Okamoto Atsushi Mukaiyama Takashi Tadokoro Dong-Ju You Hyongi Chon Yuichi Koga Kazufumi Takano Shigenori Kanaya |
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| 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 |
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| 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). |
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