Significance of Hydrophobic interaction
Hydrophobic interaction refers to the tendency of non-polar molecules to aggregate in aqueous solutions, minimizing their exposure to water. This phenomenon is crucial in various biological systems, influencing behaviors such as ligand binding to proteins, protein structure stabilization, and the behaviors of drug interactions. It plays a significant role in determining the stability and orientation of compounds within binding sites, and affects the interactions of molecules in environments like reversed-phase chromatography and molecular docking processes.
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The concept of Hydrophobic interaction in scientific sources
Hydrophobic interaction involves the tendency of non-polar molecules to avoid aqueous environments, influencing physical states, drug-protein binding stability, and polyelectrolyte properties, which are crucial for understanding molecular behavior in solutions.
(1) The lowest binding energy pose with an R-isomer of carvone demonstrated an energy of −5.03 Kcal/mol, forming a hydrogen bond interaction with Lys692 and Lys735, as well as several hydrophobic interactions with Val683, Leu853 and Leu857, as depicted in Figure 6B, describing an interaction.[1]