Thermodynamic Origin of Hofmeister Ion Effects
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A quantitative thermodynamic analysis, developed to treat noncoulombic interactions of solutes with biopolymer surface and recently extended to analyze the effects of Hofmeister salts on the surface tension of water, is applied to literature solubility data for small hydrocarbons and model peptides.Abstract:
Quantitative interpretation and prediction of Hofmeister ion effects on protein processes, including folding and crystallization, have been elusive goals of a century of research. Here, a quantitative thermodynamic analysis, developed to treat noncoulombic interactions of solutes with biopolymer surface and recently extended to analyze the effects of Hofmeister salts on the surface tension of water, is applied to literature solubility data for small hydrocarbons and model peptides. This analysis allows us to obtain a minimum estimate of the hydration b1 (H2O A−2), of hydrocarbon surface and partition coefficients Kp, characterizing the distribution of salts and salt ions between this hydration water and bulk water. Assuming that Na+ and SO42− ions of Na2SO4 (the salt giving the largest reduction in hydrocarbon solubility as well as the largest increase in surface tension) are fully excluded from the hydration water at hydrocarbon surface, we obtain the same b1 as for air-water surface (∼0.18 H2O A−2). Ran...read more
Citations
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Journal ArticleDOI
Hofmeister phenomena: an update on ion specificity in biology.
Journal ArticleDOI
Chemistry of Hofmeister anions and osmolytes.
Yanjie Zhang,Paul S. Cremer +1 more
TL;DR: A mechanism for specific ion effects is elucidated for aqueous systems containing charged and uncharged polymers, polypeptides, and proteins and a hydrogen-bonding mechanism is tested for the urea denaturation of proteins with some of these same systems.
Journal ArticleDOI
Beyond the Hofmeister Series: Ion-Specific Effects on Proteins and Their Biological Functions
Halil I. Okur,Jana Hladílková,Kelvin B. Rembert,Younhee Cho,Jan Heyda,Joachim Dzubiella,Joachim Dzubiella,Paul S. Cremer,Pavel Jungwirth +8 more
TL;DR: It is shown that the cationic and anionic Hofmeister series can now be rationalized primarily in terms of specific interactions of salt ions with the backbone and charged side chain groups at the protein surface in solution.
Journal ArticleDOI
The inverse and direct Hofmeister series for lysozyme.
Yanjie Zhang,Paul S. Cremer +1 more
TL;DR: Results suggest that in general positively charged macromolecular systems should show inverse Hofmeister behavior only at relatively low salt concentrations, but revert to a direct Hofmeisters series as the salt concentration is increased.
Journal ArticleDOI
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group
TL;DR: It is found that urea and guanidinium, although structurally similar, denature proteins by different mechanisms, and the peptide hydrogen bonding found appears sufficient to explain the thermodynamic denaturing effect of urea.
References
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How Hofmeister ion interactions affect protein stability.
TL;DR: Model compound studies in the literature show how Hofmeister ion interactions affect protein stability, and a general model, suitable for analyzing diverse ion-protein interactions, is provided by the two-domain model of Record and co-workers.
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Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated
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Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water.
Spolar Rs,Livingstone,Record Mt +2 more
TL;DR: This extension of the liquid hydrocarbon model seeks to quantify the thermodynamic contributions to protein stability from the removal of nonpolar and polar surface from water and provides a thermodynamic explanation for the observation that the specific enthalpy of folding of a number of globular proteins converges to a common value.
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