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Adachi, Motoyasu; Tamada, Taro; Kuroki, Ryota; Hidaka, Koshi*; Kimura, Toru*; Kiso, Yoshiaki*; Yamamoto, Kohei*; Kidokoro, Shunichi*
no journal, ,
no abstracts in English
Yoshimura, Naoki*; Sato, Rena*; Adachi, Motoyasu; Kuroki, Ryota; Kato, Etsuko*; Kidokoro, Shunichi*
no journal, ,
The change of the thermodynamic functions accompanying the binding of a single stranded oligo-DNA with a sequence of TCTTTTT to cold shock protein from 
HB8 was evaluated by isothermal titration calorimetry, and the three-dimensional structure of the complex was determined by X-ray crystallography. The binding was almost approximated by a two-state model and found to be stabilized by large negative enthalpy change due to the stacking interaction between the bases of the DNA and the aromatic side chains of the protein.
Adachi, Motoyasu; Shimizu, Rumi; Kuroki, Ryota; Moriya, Keisuke*; Kidokoro, Shunichi*; Hidaka, Koshi*; Tsuda, Yuko*; Kiso, Yoshiaki*
no journal, ,
Human immune deficiency virus protease-I (HIV-PR) is one of the important drug target proteins for the acquired immune deficiency syndrome. In this study, we designed the two single chain derivatives of wild-type and A17 type HIV-PRs in which the catalytic residue of Asp25 was placed with Asn25 to inactivate the enzyme. The tertiary structure of sc-HIV-PR of wild-type and A17 type were determined by X-ray crystallography to 1.1 and 1.5 
resolution, respectively. The both complex structures showed that Asn25 forms hydrogen bond with carbonyl group of inhibitor.