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The hydrophobic interaction is mostly an entropic effect originating from the disruption of the highly dynamic hydrogen bonds between molecules of liquid water by the nonpolar solute, causing the water to form a clathrate-like structure around the non-polar molecules.
Charged and polar side chains are situated on the solvent-exposed surface where they interact with surrounding water molecules. Minimizing the number of hydrophobic side chains exposed to water is the principal driving force behind the folding process, [8] [9] [10] although formation of hydrogen bonds within the protein also stabilizes protein ...
Polar molecules must contain one or more polar bonds due to a difference in electronegativity between the bonded atoms. Molecules containing polar bonds have no molecular polarity if the bond dipoles cancel each other out by symmetry. Polar molecules interact through dipole-dipole intermolecular forces and hydrogen bonds.
The hydrophobic effect represents the tendency of water to exclude non-polar 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 ...
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 ...
An example of these amphiphilic molecules is the lipids that comprise the cell membrane. Another example is soap, which has a hydrophilic head and a hydrophobic tail, allowing it to dissolve in both water and oil. Hydrophilic and hydrophobic molecules are also known as polar molecules and nonpolar molecules, respectively. Some hydrophilic ...
Hydrophobic collapse is a proposed process for the production of the 3-D conformation adopted by polypeptides and other molecules in polar solvents. The theory states that the nascent polypeptide forms initial secondary structure ( ɑ-helices and β-strands ) creating localized regions of predominantly hydrophobic residues .
Debye forces, or dipole–induced dipole interactions, can also play a role in dispersive adhesion. These come about when a nonpolar molecule becomes temporarily polarized due to interaction with a nearby polar molecule. This "induced dipole" in the nonpolar molecule then is attracted to the permanent dipole, yielding a Debye attraction.