TY - JOUR
T1 - Comparative evaluation of the stability of seven-transmembrane microbial rhodopsins to various physicochemical stimuli
AU - Honda, Naoya
AU - Tsukamoto, Takashi
AU - Sudo, Yuki
N1 - Publisher Copyright:
© 2017 Elsevier B.V.
PY - 2017
Y1 - 2017
N2 - Rhodopsins are seven-transmembrane proteins that function as photoreceptors for a variety of biological processes. Their characteristic visible colors make rhodopsins a good model for membrane-embedded proteins. In this study, by utilizing their color changes, we performed comparative studies on the stability of five microbial rhodopsins using the same instruments, procedures and media. As denaturants, we employed four physicochemical stimuli: (i) thermal perturbation, (ii) the water-soluble reagent hydroxylamine, (iii) the detergent sodium dodecyl sulfate, and (iv) the organic solvent ethanol. On the basis of the results, models for stabilization mechanisms in rhodopsins against each stimulus is proposed.
AB - Rhodopsins are seven-transmembrane proteins that function as photoreceptors for a variety of biological processes. Their characteristic visible colors make rhodopsins a good model for membrane-embedded proteins. In this study, by utilizing their color changes, we performed comparative studies on the stability of five microbial rhodopsins using the same instruments, procedures and media. As denaturants, we employed four physicochemical stimuli: (i) thermal perturbation, (ii) the water-soluble reagent hydroxylamine, (iii) the detergent sodium dodecyl sulfate, and (iv) the organic solvent ethanol. On the basis of the results, models for stabilization mechanisms in rhodopsins against each stimulus is proposed.
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U2 - 10.1016/j.cplett.2017.05.055
DO - 10.1016/j.cplett.2017.05.055
M3 - Article
AN - SCOPUS:85020164908
SN - 0009-2614
VL - 682
SP - 6
EP - 14
JO - Chemical Physics Letters
JF - Chemical Physics Letters
ER -