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Reference: Choi J, et al. (2011) Unfolding dynamics of cytochrome c revealed by single-molecule and ensemble-averaged spectroscopy. Phys Chem Chem Phys 13(13):5651-8

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Abstract


Denaturant-induced conformational change of yeast iso-1-cytochrome c (Cytc) has been comprehensively investigated in the single-molecule and bulk phases. By fluorescence-quenching experiments with dye-labelled heme-protein (Alexa 488-labelled Cytc, Cytc-A488), we clearly show that the fluorescence quenching observed from folded Cytc-A488 is due mainly to photoinduced electron transfer (PET) between electron-donating amino acids such as tryptophan and the dye attached to the protein. In addition, the unfolding process of Cytc-A488 observed in the single-molecule and bulk phases can be explained well in terms of a three-state model: Cytc unfolds through an intermediate with a native-like compactness. By quantitative analysis of fluorescence correlation spectroscopy (FCS) data, we were able to observe a relaxation time of approximately 1.5 mus corresponding to segmental motion and fast folding dynamics of 55 mus in the unfolded state of Cytc. The results presented here also suggest that a combination of single-molecule and ensemble-averaged spectroscopy is necessary to provide convincing and comprehensive assignments of protein kinetics.

Reference Type
Journal Article
Authors
Choi J, Kim S, Tachikawa T, Fujitsuka M, Majima T
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