Hydrophobicity

A result of interplay between entropy and enthalpy.

“In contrast, at the molecular scale, the driving force for hydrophobic assembly famously increases with increasing temperature. In fact, whenever biomolecular assembly occurs upon increasing temperature, in seeming disregard for entropic considerations, the hydrophobic effect is often the first suspect. A classic example is the cold denaturation of proteins. Whereas the denaturation or unfolding of proteins upon heating is common, and is ascribed to the configurational entropy of the macromolecule prevailing over the favorable energy of the folded state, certain proteins also denature upon cooling. Such cold denaturation is explained by the fact that the molecular hydrophobic effect, which stabilizes the folded state of the protein, is weakened upon cooling, causing the protein to unravel." From Xi (2016)

If I Get Time

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