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The hydrophobic effect is the observed tendency of nonpolar substances to aggregate in an aqueous solution and to be excluded by water. [ 1 ] [ 2 ] The word hydrophobic literally means "water-fearing", and it describes the segregation of water and nonpolar substances, which maximizes the entropy of water and minimizes the area of contact ...
ITC provides information regarding the stoichiometry, enthalpy, entropy, and binding kinetics between two interacting proteins. [30] Microscale thermophoresis (MST), is a new method that enables the quantitative analysis of molecular interactions in solution at the microliter scale. The technique is based on the thermophoresis of molecules ...
The effect originates from the disruption of highly dynamic hydrogen bonds between molecules of liquid water. Polar chemical groups, such as OH group in methanol do not cause the hydrophobic effect. However, a pure hydrocarbon molecule, for example hexane, cannot accept or donate hydrogen bonds to water. Introduction of hexane into water causes ...
Another related and counter-intuitive example of entropic force is protein folding, which is a spontaneous process and where hydrophobic effect also plays a role. [11] Structures of water-soluble proteins typically have a core in which hydrophobic side chains are buried from water, which stabilizes the folded state. [12]
The hydrophobic effect is the desire for non-polar molecules to aggregate in aqueous solutions in order to separate from water. [22] This phenomenon leads to minimum exposed surface area of non-polar molecules to the polar water molecules (typically spherical droplets), and is commonly used in biochemistry to study protein folding and other ...
The hydrophobic collapse introduces entropy back to the system via the breaking of the water cages which frees the ordered water molecules. [12] The multitude of hydrophobic groups interacting within the core of the globular folded protein contributes a significant amount to protein stability after folding, because of the vastly accumulated van ...
The driving mechanism for micellization is the transfer of hydrocarbon chains from water into the oil-like interior. This entropic effect is called the hydrophobic effect. Compared to the increase of entropy of the surrounding water molecules, this hydrophobic interaction is relatively small. The water molecules are highly ordered around the ...
The folding funnel hypothesis is closely related to the hydrophobic collapse hypothesis, under which the driving force for protein folding is the stabilization associated with the sequestration of hydrophobic amino acid side chains in the interior of the folded protein. This allows the water solvent to maximize its entropy, lowering the total ...