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Complete Thermal-Unfolding Profiles of Oxidized and Reduced Cytochromes c.

Authors :
Uchiyama, Susumu
Ohshima, Atsushi
Nakamura, Shota
Hsegawa, Jun
Terui, Norifumi
Takayama, Shin-ichi Joseph
Yamamoto, Yasuhiko
Sambongi, Yoshihiro
Kobayashi, Yuji
Source :
Journal of the American Chemical Society. 11/17/2004, Vol. 126 Issue 45, p14684-14685. 2p.
Publication Year :
2004

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.

Details

Language :
English
ISSN :
00027863
Volume :
126
Issue :
45
Database :
Academic Search Index
Journal :
Journal of the American Chemical Society
Publication Type :
Academic Journal
Accession number :
15261180
Full Text :
https://doi.org/10.1021/ja046667t