1. Complete Thermal-Unfolding Profiles of Oxidized and Reduced Cytochromes c.
- Author
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Uchiyama, Susumu, Ohshima, Atsushi, Nakamura, Shota, Hsegawa, Jun, Terui, Norifumi, Takayama, Shin-ichi Joseph, Yamamoto, Yasuhiko, Sambongi, Yoshihiro, and Kobayashi, Yuji
- Subjects
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PARTICLES (Nuclear physics) , *CYTOCHROMES , *BIOMOLECULES , *CYTOCHROME c , *OXIDATION-reduction reaction , *THERMODYNAMICS - Abstract
This article focuses on thermal unfolding profiles. An electron-transfer protein, soluble monoheme cytochrome c (cyt c) is among the essential redox proteins sustaining biological activity. Another fundamental way to elucidate the redox function of cyt c is to characterize its thermo-dynamic property of both oxidized and reduced forms because the redox potential is derived from the difference between these two redox states. Conventionally, there are two protein thermal-unfolding experiments. First, differential scanning calorimetric (DSC) measurements can be carried out at more than 100 degree celcius.
- Published
- 2004
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