Role of cooperativity in hydrophobic interactions revealed in real-time monitoring

Hydrophobic interactions is one major type of intermolecular force that plays a vital role in many life processes in Chemistry and Physics. In biological systems, hydrophobic interactions can stabilize the internal cores of proteins and form lipid vesicles that store nutrients in our cells.In proteins, hydrophobic interactions can stabilize the internal cores and form lipid vesicles that store nutrients in our cells.What is so intriguing about hydrophobic interaction is that it exhibits a cooperative property called cooperativity, which does not exist in other fundamental intermolecular forces, such as dipole-dipole interactions and Van der Waals forces. Cooperativity means that in the presence of multiple molecules (at least more than two), the overall strength of the interaction between the molecules is much greater than that when there are only two molecules acting in pairs.