Biology · Biochemistry

The following experimental observations are made when a small ligand binds with nanomolar affinity in a deep hydrophobic pocket of the partner protein: A. The ligand forms a hydrogen bond with a backbone carbonyl oxygen upon binding. B. Several nonpolar groups in proteins form a hydrophobic network due to the conformational change, leading to the displacement of buried water molecules to the surface. C. A negatively charged side chain of an amino acid located near the binding site is desolvated. D. The desolvated sidechain of an amino acid located near the binding site does not form a salt bridge with the ligand. Which one of the following options represents the combination of all correct statement(s) that explain(s) net stabilisation of the ligand:protein complex?