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Counteraction of denaturant-induced protein unfolding is a general property of stabilizing agents

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Abstract

DSC measurements on RNase A at neutral pH show that five stabilizing agents, namely trimethylamine N-oxide, glucose, sucrose, betaine and sodium sulfate, can counteract the destabilizing action of urea, sodium perchlorate, guanidinium chloride and guanidinium thiocyanate. This is an important finding inferring that counteraction has a common physical origin, regardless of the chemical differences among the stabilizing agents and among the destabilizing ones. A rationalization is provided grounded on the following line of reasoning: (a) the decrease in solvent-excluded volume effect is the main stabilizing contribution of the native state; (b) its magnitude increases on increasing the density of the aqueous solution; (c) the density increases significantly in the ternary solutions containing water, a stabilizing agent and a destabilizing one, as indicated by the present experimental data.

Graphical abstract: Counteraction of denaturant-induced protein unfolding is a general property of stabilizing agents

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Publication details

The article was received on 12 Jul 2018, accepted on 07 Nov 2018 and first published on 07 Nov 2018


Article type: Paper
DOI: 10.1039/C8CP04421J
Citation: Phys. Chem. Chem. Phys., 2018, Advance Article
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    Counteraction of denaturant-induced protein unfolding is a general property of stabilizing agents

    S. Cozzolino, R. Oliva, G. Graziano and P. Del Vecchio, Phys. Chem. Chem. Phys., 2018, Advance Article , DOI: 10.1039/C8CP04421J

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