Tracking the chiral recognition of adsorbed dipeptides at the single-molecule level

Specific molecular recognition depends on the precisely defined arrangement of atoms in complementary structures interacting by short-range forces. The mutual interactions between complementary molecules can result in their recognition even if their static molecular structure is not optimized for specific binding. This mechanism of dynamic induced fit, orginally introduced by Pauling in 1948 and developed by Koshland for enzymatic activity, is today the generally accepted picture in biomolecular recognition processes.