Figure 4. Importance of dynamics in protein-ligand interactions.

(A) The conformational equilibrium revealed by NMR explains the conformational entropy gain coupled to binding a ligand in multidrug binding transcription factor, LmrR. The population shift upon ligand binding correlates with the conformational entropy gain calculated from the changes in fast methyl dynamics (for detail see ref¹¹³) (B) The coupling between compound binding and enhancement of methyl dynamics in hydrophobic core. The upper displacement of the C-helix caused by compound binding loosens the hydrophobic core beneath the helix.