Results 251 to 260 of about 755,747 (299)
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Hydrophobic Volume Effects in Albumin Solutions
Journal of Colloid and Interface Science, 2001Density measurements of aqueous albumin solutions as a function of concentration and temperature are reported. The solvents were H(2)O, D(2)O, and a physiological H(2)O-based buffer. An anomaly of the density at very small concentrations of albumin in D(2)O was found.
Schrade, P. +4 more
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Current Opinion in Structural Biology, 1991
Abstract This review discusses three developments: advances in the random network model of water, which provide a better understanding of water's unique thermodynamic properties; thermodynamic analyses of hydrophobic solvation, which illuminate the role of enthalpic and entropic effects; and, direct measurements, using site-directed mutagenesis, of ...
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Abstract This review discusses three developments: advances in the random network model of water, which provide a better understanding of water's unique thermodynamic properties; thermodynamic analyses of hydrophobic solvation, which illuminate the role of enthalpic and entropic effects; and, direct measurements, using site-directed mutagenesis, of ...
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The hydrophobic effect in protein folding
The FASEB Journal, 1995In this review of protein folding we consider the noncovalent interactions existing between atoms or molecules at the molecular level. The electrostatic, Van dcr Waals, hydrogen bonding, and hydrophobic interactions are described and their contribution to protein conformation is discussed.
Lins, Laurence, Brasseur, Robert
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Curvature effects on hydrophobic solvation
Molecular Physics, 1996Molecular dynamics simulations were performed on four systems: pure SPC/E water, and three solutes with different surface curvatures in water. The same intermolecular potential was employed throughout, but the radius of curvature was altered by inserting a hard ‘inner core’ into the solute. The radial distribution function, angular distribution, a bond-
P.-L. CHAU, T.R. FORESTER, W. SMITH
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Lyotropic salt effects in hydrophobic chromatography
Analytical Biochemistry, 1975Abstract Pure hydrophobic chromatography can be observed with agarose gels containing caprylyl hydrazide. These nonionic gels show increased avidity in protein adsorption with higher content of caprylyl groups. Lyotropic salt effects can be used to control chromatographic behavior of proteins. Salting-out agents enhance binding of protein to sorbent,
A H, Nishikawa, P, Bailon
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Current Opinion in Colloid & Interface Science, 2016
Abstract This review is a brief discussion on the development of the understanding of hydrophobicity, or the hydrophobic effect. The hydrophobic effect is primarily discussed in terms of partitioning of hydrocarbons between a hydrophobic environment and water as well as solubility of hydrocarbons in water. Micellization of surfactants is only briefly
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Abstract This review is a brief discussion on the development of the understanding of hydrophobicity, or the hydrophobic effect. The hydrophobic effect is primarily discussed in terms of partitioning of hydrocarbons between a hydrophobic environment and water as well as solubility of hydrocarbons in water. Micellization of surfactants is only briefly
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Hydrophobic effects on partial molar volume
The Journal of Chemical Physics, 2005The hydrophobic effects on partial molar volume (PMV) are investigated as a PMV change in the transfer of a benzenelike nonpolar solute from the nonpolar solvent to water, using an integral equation theory of liquids. The volume change is divided into two effects.
Takashi, Imai, Fumio, Hirata
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The hydrophobic effect: a reappraisal
Pure and Applied Chemistry, 1989Abstract
P. L. Privalov, S. J. Gill
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Annual Review of Physical Chemistry, 1985
The subject of this review is the solution environment of nonpolar molecules dissolved in liquid water, and the molecular description of the most likely encounters between such solutes in aqueous solution. These subjects have been traditionally discussed under the name, "hydrophobic effects." Several reviews have been written previously about ...
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The subject of this review is the solution environment of nonpolar molecules dissolved in liquid water, and the molecular description of the most likely encounters between such solutes in aqueous solution. These subjects have been traditionally discussed under the name, "hydrophobic effects." Several reviews have been written previously about ...
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Theory of the hydrophobic effect
The Journal of Chemical Physics, 1977A microscopic theory is developed which can describe many of the structural and thermodynamic properties of infinitely dilute solutions of apolar solutes in liquid water. The theory is based on an integral equation for the pair correlation functions associated with spherical apolar species dissolved in water.
Lawrence R. Pratt, David Chandler
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