ニュース

「Biophysics and Physicobiology」にShohei Konno et al. “Uncovering dehydration in cytochrome c refolding from urea- and guanidine hydrochloride-denatured unfolded state by high pressure spectroscopy”を掲載

2019年02月01日 学会から

日本生物物理学会欧文誌[Biophysics and Physicobiology]に以下の論文が新規掲載されました。

Shohei Konno, Kentaro Doi, Koichiro Ishimori “Uncovering dehydration in cytochrome c refolding from urea- and guanidine hydrochloride-denatured unfolded state by high pressure spectroscopy”

【Significance】
Uncovering dehydration in cytochrome c by high pressure spectroscopy

The high pressure absorption spectroscopy revealed that the partial volume changes for the unfolding of cytochrome c (Cyt c) to the urea- and guanidine hydrochloride (GdnHCl)-denatured unfolded states (ΔVu) were positive, reflecting hydration to hydrophobic heme; however, a more positively shifted ΔVu was observed for urea-denatured Cyt c. Introduction of the mutation near the axial ligand induced more drastic changes in the hydrated structure of the urea-denatured Cyt c, suggesting that the hydrated structure in the unfolded state depends on the denaturant. Our approach enables us to examine the dehydration associated with protein folding and hydration structures in the unfolded states.


Biophysics and Physicobiology, Vol.16, pp. 18-27URL:https://doi.org/10.2142/biophysico.16.0_18


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