Coherent Signal Picks Out Biomolecular Interactions

11. August 2014

Gerd Binnig, Physics 7, 84 (2014)

Proteins rarely act alone: Their functioning requires that they establish contact with other proteins and molecules, mostly through noncovalent interactions (i.e., interactions that do not involve the sharing of electrons, such as hydrogen-bond and van der Waals interactions). The study of such interactions is key for the understanding of biology at the molecular level, and may have important implications for drug discovery or the development of diagnostic tests. It is thus crucial to develop measurement techniques that can selectively probe these interactions, characterizing, for instance, the formation rate and strength of a specific protein-ligand complex, while discriminating from other, nonspecific interactions (like those arising, for instance, between a protein and fluctuating solute molecules). Writing in Physical Review X, Christof Fattinger, of Roche Innovation Center, Basel, Switzerland, investigates theoretically a novel analytical method, called focal “molography” (molecular holography), which represents a potential breakthrough for the selective detection of molecular interactions.