Introduction
CD spectra provide information on the secondary structure of proteins and the environment of
aromatic side chains. Therefore, CD measurement using a stopped-flow system is considered as one of
the best methods for analyzing the unfolding and refolding of proteins.
The existence of an intermediate between denaturated state and natural state during the refolding of
proteins has been reported. The CD stopped-flow method is used for examining this refolding process. In
this report the refolding process of cytochrome c (cyt c) measured using a SFS-492 stopped-flow system
will be explained.
Keywords: Stopped-flow, Circular Dichroism, Refolding
Sample Preparation
Aqueous solution of Cytochrome c denaturated by guanidine hydrochloride (GuHCl) was diluted with
0.1 M acetic acid buffer solution (1:9). The refolding process was observed at 222 nm for the secondary JASCO圆二色光谱仪CD J-1500
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