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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.
A hydrophilic molecule or portion of a molecule is one whose interactions with water and other polar substances are more thermodynamically favorable than their interactions with oil or other hydrophobic solvents. [2] [3] They are typically charge-polarized and capable of hydrogen bonding.
The hydrophobic effect depends on the temperature, which leads to "cold denaturation" of proteins. [19] The hydrophobic effect can be calculated by comparing the free energy of solvation with bulk water. In this way, the hydrophobic effect not only can be localized but also decomposed into enthalpic and entropic contributions. [3]
Non-covalent interactions can be classified into different categories, such as electrostatic, π-effects, van der Waals forces, and hydrophobic effects. [3] [2] Non-covalent interactions [4] are critical in maintaining the three-dimensional structure of large molecules, such as proteins and nucleic acids.
Biological molecules are amphiphilic or amphipathic, i.e. are simultaneously hydrophobic and hydrophilic. [6] The phospholipid bilayer contains charged hydrophilic headgroups, which interact with polar water. The layers also contain hydrophobic tails, which meet with the hydrophobic
This difference is due to the different methods used to measure hydrophobicity. The method used to obtain the Janin and Rose et al. scales was to examine proteins with known 3-D structures and define the hydrophobic character as the tendency for a residue to be found inside of a protein rather than on its surface.
Accordingly, one can think of the driving force of these interactions as the minimization of total interfacial free energy, i.e. minimization of surface area. [10] Illustration of how protein changes shape to allow polar regions (blue) to interact with water while non-polar hydrophobic regions (red) do not interact with the water.
The hydrophilic end usually contains a negatively charged phosphate group, and the hydrophobic end usually consists of two "tails" that are long fatty acid residues. [ 4 ] In aqueous solutions, phospholipids are driven by hydrophobic interactions , which result in the fatty acid tails aggregating to minimize interactions with the water molecules.