Kishimoto Ayaka | Grad. Sch. Sci. Univ. Hyogo
スポンサーリンク
概要
関連著者
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Kishimoto Ayaka
Grad. Sch. Sci. Univ. Hyogo
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Shimada Hideo
Grad. Sch. Life Sci., Univ. Hyogo
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Hayashi Takashi
Grad. Sch. Eng. Osaka Univ.
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Mizushima Tsunehiro
Grad. Sch. Sci., Univ. Hyogo
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Sakurai Keisuke
Inst. Sci. Ind. Res., Osaka Univ.
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Takagi Kenji
Grad. Sch. Sci., Univ. Hyogo
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Shimada Hideo
Grad. Sch. Sci. Univ. Hyogo
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Harada Katsuyoshi
Grad. Sch. Eng. Osaka Univ.
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Hayashi Takashi
Grad. Sch. Eng., Osaka Univ.
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Sugiyama Hidehisa
Grad. Sch. Life Sci. Univ. Hyogo
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Shimada Hideo
Picobiology Institute Graduate School Of Life Science University Of Hyogo
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Harada Katsuyoshi
Department Of Applied Chemistry Graduate School Of Engineering Osaka University
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Fujii Rie
Picobiology Institute Graduate School Of Life Science University Of Hyogo
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Kunitoshi Shimokata
World Intec Co. Ltd.
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Shimokata Kunitoshi
World Intec Co. Ltd.
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Sakurai Keisuke
Picobiology Institute Graduate School Of Life Science University Of Hyogo
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Fujii Rie
Grad. Sch. Sci. Univ. Hyogo
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Sakurai Keisuke
Grad. Sch. Sci. Univ. Hyogo
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Kitamura Natsumi
Grad. Sch. Sci. Univ. Hyogo
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Amano Aya
Grad. Sch. Sci., Univ. Hyogo
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Shimada Hideo
Grad. Sch. Sci., Univ. Hyogo
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Muramoto Kazumasa
Grad. Sch. Life Sci., Univ. Hyogo
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Kitamura Natsumi
Grad. Sch. Sci., Univ. Hyogo
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Harada Katsuyoshi
Grad. Sch. Eng., Osaka Univ.
著作論文
- 2I1548 Reaction of norcamphor with cytochrome P450cam mutated at the gate forming Asp297 for putative water expelling pathway(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
- 2I1536 Water expelling pathway of cytochrome P450cam : Effect of mutation of a gate forming Asp297 to Leu on D-camphor binding(Heme proteins 2,The 48th Annual Meeting of the Biophysical Society of Japan)
- 2PT164 Norcamphor binding to cytochrome P450cam with a mutation to block pathway for the active site waters excluded by substrate(The 50th Annual Meeting of the Biophysical Society of Japan)
- 2PT162 Exclusion of the active site waters by substrate in cytochrome P450cam(The 50th Annual Meeting of the Biophysical Society of Japan)
- 1P096 Heme serves as scaffold for substrate-driven active site structuring in cytochrome P450cam(02. Heme proteins,Poster)
- 1P095 Substrate access to slow substrate binding P450cam with mutation at the proposed gate for water egress/ingress from/to the active site(02. Heme proteins,Poster)