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Electrodynamic pressure modulation of protein stability in cosolvents.
- Source :
-
Biochemistry [Biochemistry] 2013 Nov 19; Vol. 52 (46), pp. 8363-73. Date of Electronic Publication: 2013 Nov 07. - Publication Year :
- 2013
-
Abstract
- Cosolvents affect structural stability of proteins in aqueous solutions. A clear understanding of the mechanism by which cosolvents impact protein stability is critical to understanding protein folding in a biological milieu. In this study, we investigated the Lifshitz-van der Waals dispersion interaction of seven different solutes with nine globular proteins and report that in an aqueous medium the structure-stabilizing solutes exert a positive electrodynamic pressure, whereas the structure-destabilizing solutes exert a negative electrodynamic pressure on the proteins. The net increase in the thermal denaturation temperature (ΔTd) of a protein in 1 M solution of various solutes was linearly related to the electrodynamic pressure (PvdW) between the solutes and the protein. The slope of the PvdW versus ΔTd plots was protein-dependent. However, we find a positive linear relationship (r(2) = 0.79) between the slope (i.e., d(ΔTd)/dPvdW) and the adiabatic compressibility (βs) of the proteins. Together, these results clearly indicate that the Lifshitz's dispersion forces are inextricably involved in solute-induced stabilization/destabilization of globular proteins. The positive and/or negative electrodynamic pressure generated by the solute-protein interaction across the water medium seems to be the fundamental mechanism by which solutes affect protein stability. This is at variance with the existing preferential hydration concept. The implication of these results is significant in the sense that, in addition to the hydrophobic effect that drives protein folding, the electrodynamic forces between the proteins and solutes in the biological milieu also might play a role in the folding process as well as in the stability of the folded state.
- Subjects :
- Amino Acids pharmacology
Calorimetry, Differential Scanning
Chymotrypsinogen chemistry
Conalbumin chemistry
Lactalbumin chemistry
Lactoglobulins chemistry
Muramidase chemistry
Myoglobin chemistry
Ovalbumin chemistry
Ovomucin chemistry
Polyethylene Glycols pharmacology
Pressure
Protein Denaturation
Protein Folding
Ribonuclease, Pancreatic chemistry
Sucrose pharmacology
Temperature
Urea pharmacology
Water chemistry
Electromagnetic Phenomena
Protein Stability
Solutions chemistry
Solvents chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1520-4995
- Volume :
- 52
- Issue :
- 46
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 24156352
- Full Text :
- https://doi.org/10.1021/bi400656a