Book•
The Hydrophobic Effect: Formation of Micelles and Biological Membranes
01 Aug 1991-
TL;DR: In this article, the authors discuss the properties of water molecules and their relationship with common soluble proteins, such as membrane proteins and membrane membrane proteins, as well as the effect of temperature on their properties.
Abstract: The Solubility of Hydrocarbons in Water. Solubility of Amphiphiles in Water and Organic Solvents. The Effect of Temperature: Anomalous Entropy and Heat Capacity. The Structure of Water. Micelles: Introduction. Thermodynamics of Micelle Formation. Micelle Size and Shape. Mixed Micelles. Monolayers. Biological Lipids. Motility and Order. Proteins: Hydrophobic Side Chains and Conformational Change. The Association of Hydrocarbons and Amphiphiles with Common Soluble Proteins. Serum Lipoproteins. Biological Membranes. Membrane Proteins. Author and Subject Indices.
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15,091 citations
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TL;DR: A coherent thermodynamic formalism for determining and describing the energetics of peptide-bilayer interactions and a review of the properties of the environment of membrane proteins--the bilayer milieu are reviewed.
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1,703 citations
TL;DR: In this paper, the authors developed a unified and generally applicable theory of solvation of small and large apolar species in water, where hydrogen bonding of water is hindered yet persists near the solutes, leading to drying of extended apolar surfaces, large forces of attraction and hysteresis on mesoscopic length scales.
Abstract: We develop a unified and generally applicable theory of solvation of small and large apolar species in water. In the former, hydrogen bonding of water is hindered yet persists near the solutes. In the latter, hydrogen bonding is depleted, leading to drying of extended apolar surfaces, large forces of attraction, and hysteresis on mesoscopic length scales. The crossover occurs on nanometer length scales, when the local concentration of apolar units is sufficiently high, or when an apolar surface is sufficiently large. Our theory for the crossover has implications concerning the stability of protein assemblies and protein folding.
1,535 citations
TL;DR: It is found that solvent properties of water within the interphase separating a solid surface from bulk water solution vary with contacting surface chemistry, and this interphase can extend tens of nanometers from a water-contacting surface due to a propagation of differences in self association between vicinal water and bulk-phase water.
1,396 citations