シトクロムcモルテングロビュール状態に関する熱力学的研究
書誌事項
- タイトル別名
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- Thermodynamic Study on the molten globule state of cytochrome c
抄録
Molten globule (MG) state, which is structurally distinct from both the native (N) and denatured (D) states, was originally proposed as an equilibrium intermediate state of denaturation of some proteins with a compact conformation, a considerable native-like secondary structure, and a largely fluctuating tertiary structure. Recently, our group has developed isothermal acid-titration calorimetry (IATC), a calorimetric method for evaluating the enthalpy change accompanying the pH-induced transition of protein using isothermal titration calorimeter. By this method, the pH-induced transition from N to MG state of cytochrome c was directly observed by calorimetry and was confirmed to be a two-state transition with small enthalpy change. Also, the MG state was detected in the thermal transition from N to D state by highly precise differential scanning calorimetry.
収録刊行物
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- 熱測定
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熱測定 34 (3), 113-119, 2007
日本熱測定学会
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キーワード
詳細情報 詳細情報について
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- CRID
- 1390282680066771584
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- NII論文ID
- 130003658858
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- ISSN
- 18841899
- 03862615
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- 本文言語コード
- ja
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- データソース種別
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- JaLC
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可