biophysics said:
Hydrophobicity refers to the tendency of a molecule or substance to repel or not mix with water. This is due to the molecule's nonpolar nature and lack of affinity for water molecules.
Hydrogen bonding is a type of intermolecular force that occurs between polar molecules. In hydrophobic interactions, nonpolar molecules cluster together to avoid contact with water, while polar water molecules form hydrogen bonds with each other. This results in a decrease in the overall free energy of the system.
Hydrophobic interactions play a crucial role in protein folding, as the hydrophobic amino acid side chains tend to cluster together in the interior of the protein, away from water molecules. This helps to stabilize the protein's structure and allows it to fold into its functional shape.
No, hydrophobic molecules cannot form hydrogen bonds with water because they lack polar groups or atoms that can participate in hydrogen bonding. Instead, they form van der Waals interactions with water molecules.
Hydrophobic interactions can be disrupted by the addition of polar molecules, such as detergents or salts, which can interact with the hydrophobic molecules and disrupt their clustering. This can lead to changes in the structure and function of proteins and other biomolecules.