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Journal ArticleDOI

Solute‐Solute Interactions in Aqueous Solutions

John J. Kozak, +2 more
- 15 Jan 1968 - 
- Vol. 48, Iss: 2, pp 675-690
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TLDR
In this article, the authors interpreted solvent-solute interactions in aqueous solutions of nonelectrolytes using both lattice and distribution function theories of the dissolved state.
Abstract
Solute‐solute interactions in aqueous solutions of nonelectrolytes are interpreted using both lattice and distribution function theories of the dissolved state. Experimental activity data of high precision can be obtained from the literature for aqueous solutions of many nonelectrolytes. If the logarithm of the solvent activity coefficient (γ1) is expressed as a power series in the mole fraction of the solute (x2), lnγ1 = Bx22 + Cx23 + ···, then the coefficients B and C can be determined analytically from the experimental measurements. Values of B were obtained for 52 aqueous mixtures; values of C were obtained for 39 of these mixtures. The solutes considered include aliphatic alcohols, amines, amides, ketones, fatty acids, amino acids, and sugars. In some cases, experimental data were available from which the temperature dependence of the quantities B and C could also be determined. The effect of solute size on the coefficients B and C was investigated using the lattice theories of Flory, Huggins, and Gu...

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Citations
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Lewis-Randall to McMillan-Mayer conversion for the thermodynamic excess functions of solutions. Part I. Partial free energy coefficients

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The effect of polyhydric and monohydric alcohols on the heat-induced reversible denaturation of lysozyme and ribonuclease.

TL;DR: The reversible thermal denaturation of lysozyme and ribonuclease was investigated in aqueous solutions of mono- and polyvalent alcohols and it was reasoned that these stabilizing effects may find their origin in the intensification of the intra-hydrophobic interactions of the protein.
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Hydrophobe Effekte – Ansichten und Tatsachen

TL;DR: In this article, a ubersicht beschreibt einige neue Erkenntnisse aus den letzten zehn Jahren, e.g., Enzym-Substrat-Wechselwirkungen, the Anordnung von Lipiden in biologischen Membranen, Aggregation oberflachenaktiver Stoffe and kinetische Solvenseffekte in wasserreichen Losungsmittelsystemen.
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Solvent effects on protein association and protein folding

TL;DR: The findings lead to the conclusion that the currently used hydrophobicity scales, based on partition coefficients between water and an organic solvent, are inadequate measures of the contribution of side chains being transferred from water to the interior of the protein.
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Effects of solute--solvent attractive forces on hydrophobic correlations

TL;DR: In this paper, a theory for the effect of slowly varying attractive forces on correlations between nonpolar solutes in dilute aqueous solution is presented, and it is shown that hydrophobic correlations are sensitive to relatively long range slowly varying interactions.
References
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Book

Molecular theory of gases and liquids

TL;DR: Molecular theory of gases and liquids as mentioned in this paper, molecular theory of gas and liquids, Molecular theory of liquid and gas, molecular theories of gases, and liquid theory of liquids, مرکز
Book ChapterDOI

Some factors in the interpretation of protein denaturation.

TL;DR: The chapter reviews that the denaturation is a process in which the spatial arrangement of the polypeptide chains within the molecule is changed from that typical of the native protein to a more disordered arrangement.
Journal ArticleDOI

Thermodynamics of High Polymer Solutions

TL;DR: In this paper, a statistical treatment of high polymer solutions has been carried out on the basis of an idealized model, originally proposed by Meyer, which is analogous to the one ordinarily assumed in the derivation of the ''ideal'' solution laws for molecules of equal size.
Journal ArticleDOI

Free Volume and Entropy in Condensed Systems III. Entropy in Binary Liquid Mixtures; Partial Molal Entropy in Dilute Solutions; Structure and Thermodynamics in Aqueous Electrolytes

TL;DR: The first and second papers in this series, which make it possible to interpret entropy data in terms of a physical picture, are applied to binary solutions, and equations are derived relating energy and volume changes when a solution is formed to the entropy change for the process as discussed by the authors.
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