Thermodynamic Study on the molten globule state of cytochrome c
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- Nakamura Shigeyoshi
- Dept. of Bioengineering, Nagaoka Univ. of Technology
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- Kidokoro Shun-ichi
- Dept. of Bioengineering, Nagaoka Univ. of Technology
Bibliographic Information
- Other Title
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- 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
Abstract
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.
Journal
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- Netsu Sokutei
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Netsu Sokutei 34 (3), 113-119, 2007
The Japan Society of Calorimetry and Thermal Analysis
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Keywords
Details 詳細情報について
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- CRID
- 1390282680066771584
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- NII Article ID
- 130003658858
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- ISSN
- 18841899
- 03862615
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- Text Lang
- ja
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- Data Source
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- JaLC
- CiNii Articles
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- Abstract License Flag
- Disallowed