Issue 8, 2012

On the effect of low concentrations of alcohols on the conformational stability of globular proteins

Abstract

Low concentrations of alcohols have proven to be able to enlarge the stability curve of globular proteins, by decreasing the cold denaturation temperature and increasing the hot denaturation temperature [S. R. Martin, V. Esposito, P. De Los Rios, A. Pastore and P. A. Temussi, J. Am. Chem. Soc., 2008, 130, 9963–9970]. In order to try to explain these data, I have considered that: (1) an aqueous 2 M MeOH solution can be treated as a uniform liquid, constituted by water molecules, whose density, above the temperature of maximum density, has the same values of neat water, simply shifted by 2 °C toward lower temperatures, whereas, below the temperature of maximum density, it decreases to a slightly lesser extent than the density of neat water; (2) the ΔEa(2 M MeOH) quantity, a balance between intra-protein energetic attractions and those with the surrounding solvent molecules, both water and methanol, assumes a constant positive value. These physically-based assumptions, when inserted into the theoretical model developed to rationalize the occurrence of cold denaturation in neat water [G. Graziano, Phys. Chem. Chem. Phys., 2010, 12, 14245–14252], reproduce in a qualitatively correct manner the effect of low concentrations of alcohols.

Graphical abstract: On the effect of low concentrations of alcohols on the conformational stability of globular proteins

Supplementary files

Article information

Article type
Paper
Submitted
03 Nov 2011
Accepted
03 Jan 2012
First published
05 Jan 2012

Phys. Chem. Chem. Phys., 2012,14, 2769-2773

On the effect of low concentrations of alcohols on the conformational stability of globular proteins

G. Graziano, Phys. Chem. Chem. Phys., 2012, 14, 2769 DOI: 10.1039/C2CP23463G

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