Event

A Nonequilibrium Approach to Allosteric Communication

Peter Hamm, Department of Chemistry, University of Zurich, Switzerland

With the term allostery one describes the coupling of two separated sites of a protein, where binding of a ligand at the so-called allosteric site changes the function of the protein at a remote active site. Allostery is one of the fundamental mechanisms of regulatory processes in life. The very question of how these two sites communicate with each other remains an intriguing and controversial problem, with the ultimate question of how an allosteric signal propagates through a protein.

Transient IR spectroscopy provides the time resolution combined with the chemical selectivity necessary to study these nonequilibrium processes. In these experiments, an allosteric protein is light-trigger with the help of a photo-isomerizing azobenzene moiety, which is incorporated into the protein in a way that it mimics an allosteric process, and the response of the protein is recorded by transient IR spectroscopy. I will discuss a variety of protein systems that we have designed for that purpose, as well as ongoing experiments.