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- W2124460503 abstract "Ribonuclease HII from hyperthermophile Thermococcus kodakaraensis (Tk-RNase HII) is a robust monomeric protein under kinetic control, which possesses some proline residues at the N-terminal of α-helices. Proline residue at the N-terminal of an α-helix is thought to stabilize a protein. In this work, the thermostability and folding kinetics of Tk-RNase HII were measured for mutant proteins in which a proline residue is introduced (Xaa to Pro) or removed (Pro to Ala) at the N-terminal of α-helices. In the folding experiments, the mutant proteins examined exhibit little influence on the remarkably slow unfolding of Tk-RNase HII. In contrast, E111P and K199P exhibit some thermostabilization, whereas P46A, P70A and P174A have some thermodestabilization. E111P/K199P and P46A/P70A double mutations cause cumulative changes in stability. We conclude that the proline effect on protein thermostability is observed in a hyperthermophilic protein, but each proline residue at the N-terminal of an α-helix slightly contributes to the thermostability. The present results also mean that even a natural hyperthermophilic protein can acquire improved thermostability." @default.
- W2124460503 created "2016-06-24" @default.
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- W2124460503 date "2008-10-25" @default.
- W2124460503 modified "2023-09-27" @default.
- W2124460503 title "Proline Effect on the Thermostability and Slow Unfolding of a Hyperthermophilic Protein" @default.
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- W2124460503 doi "https://doi.org/10.1093/jb/mvn144" @default.
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