Inside Cover: Microsecond Timescale Conformational Dynamics of a Small‐Molecule Ligand within the Active Site of a Protein (Angew. Chem. Int. Ed. 5/2024)

Graphical Abstract Round and round The intrinsic dynamics of small-molecule ligands while bound to their protein targets is of interest for optimization of the entropic contributions to binding affinity. In their Communication (e202313947), Rasmus Linser et al. show that NMR proton relaxation dispersion is able to capture an aromatic ring flip within a high-affinity pharmacological inhibitor on the µs timescale.