Thermodynamic Origin of Hofmeister Ion Effects
作者： Laurel M. Pegram , M. Thomas Record
DOI: 10.1021/JP800816A
关键词: Crystallization 、 Ion 、 Partition coefficient 、 Solubility 、 Surface tension 、 Salt (chemistry) 、 Physical chemistry 、 Molecule 、 Chemistry 、 Hofmeister series 、 Thermodynamics
摘要: Quantitative interpretation and prediction of Hofmeister ion effects on protein processes, including folding crystallization, have been elusive goals a century research. Here, quantitative thermodynamic analysis, developed to treat noncoulombic interactions solutes with biopolymer surface recently extended analyze the salts tension water, is applied literature solubility data for small hydrocarbons model peptides. This analysis allows us obtain minimum estimate hydration b1 (H2O A−2), hydrocarbon partition coefficients Kp, characterizing distribution salt ions between this water bulk water. Assuming that Na+ SO42− Na2SO4 (the giving largest reduction in as well increase tension) are fully excluded from at surface, we same air-water (∼0.18 H2O A−2). Ran...
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M. Thomas Record, Wentao Zhang, Charles F. Anderson, Analysis of effects of salts and uncharged solutes on protein and nucleic acid equilibria and processes: a practical guide to recognizing and interpreting polyelectrolyte effects, Hofmeister effects, and osmotic effects of salts. Advances in Protein Chemistry. ,vol. 51, pp. 281- 353 ,(1998) , 10.1016/S0065-3233(08)60655-5
Serge N. Timasheff, Control of Protein Stability and Reactions by Weakly Interacting Cosolvents: The Simplicity of the Complicated Advances in Protein Chemistry. ,vol. 51, pp. 355- 432 ,(1998) , 10.1016/S0065-3233(08)60656-7
Daniel J. Felitsky, Jonathan G. Cannon, Michael W. Capp, Jiang Hong, Adam W. Van Wynsberghe, Charles F. Anderson, M. Thomas Record, The exclusion of glycine betaine from anionic biopolymer surface: why glycine betaine is an effective osmoprotectant but also a compatible solute. Biochemistry. ,vol. 43, pp. 14732- 14743 ,(2004) , 10.1021/BI049115W
Tsutomu Arakawa, Serge N. Timasheff, Preferential interactions of proteins with salts in concentrated solutions Biochemistry. ,vol. 21, pp. 6545- 6552 ,(1982) , 10.1021/BI00268A034
Jonathan G. Cannon, Charles F. Anderson, M. Thomas Record, Urea-amide preferential interactions in water: quantitative comparison of model compound data with biopolymer results using water accessible surface areas. Journal of Physical Chemistry B. ,vol. 111, pp. 9675- 9685 ,(2007) , 10.1021/JP072037C
Samuel Glasstone, Denys W. Dimond, Edward C. Jones, CCCXCI.—Solubility influences. Part II. The effect of various salts on the solubility of ethyl acetate in water J. Chem. Soc.. ,vol. 129, pp. 2935- 2939 ,(1926) , 10.1039/JR9262902935
Dominik Horinek, Roland R. Netz, Specific ion adsorption at hydrophobic solid surfaces. Physical Review Letters. ,vol. 99, pp. 226104- 226104 ,(2007) , 10.1103/PHYSREVLETT.99.226104
Peter H. Von Hippel, Thomas Schleich, Ion effects on the solution structure of biological macromolecules Accounts of Chemical Research. ,vol. 2, pp. 257- 265 ,(1969) , 10.1021/AR50021A001
Jiang Hong, Mike W. Capp, Ruth M. Saecker, M. Thomas Record, Use of Urea and Glycine Betaine To Quantify Coupled Folding and Probe the Burial of DNA Phosphates in Lac Repressor−Lac Operator Binding† Biochemistry. ,vol. 44, pp. 16896- 16911 ,(2005) , 10.1021/BI0515218
Katsuhiko Deguchi, Kenjiro Meguro, The effects of inorganic salts and urea on the micellar structure of nonionic surfactant Journal of Colloid and Interface Science. ,vol. 50, pp. 223- 227 ,(1975) , 10.1016/0021-9797(75)90224-6