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Báo cáo khoa học: Solution structure and stability of the full-length excisionase from bacteriophage HK022

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:13

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Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisi-onase protein (Xis)from thek-like bacteriophage HK022 and to study its sequence-specificDNA interaction. Aswild-typeXiswas previously characterizedas a generallyunstable protein, abiologicallyactiveHK022Xismutantwithasingle amino acid substitutionCys28fiSerwas used in this work. This substitution has been shown to diminish the irreversi-bility of Xis denaturation and subsequent degradation, but does not affect the structural or thermodynamic properties of the protein, as evidenced by NMR and differential scan-ning calorimetry. ...

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Nội dung Text: Báo cáo khoa học: Solution structure and stability of the full-length excisionase from bacteriophage HK022

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