Date: 05.05..2023, Time: 15:30h

Location: Kleiner Physikhörsaal N020, Fakultät für Physik
The talk will also be streamed online.

Dr. Thomas Weikl
Max Planck Institute of Colloids and Interfaces, Department of Biomolecular Systems, Potsdam

Recognition of molecular binding partners is crucial for all biological process and typically requires a certain shape complementarity between partners, as emphasized in the "lock and key" notion of binding. Two important aspects in molecular recognition beyond lock and key are: (1) many proteins change their shape during binding, e.g. in allosteric signaling, and (2) recognition events at cell-cell interfaces occur only at sufficiently close cell contacts. In my talk, I will address these aspects from a modeling perspective. A central question is how protein shape changes are coupled to binding, and whether a shape change occurs predominantly prior to a binding event ("conformational selection"), or after binding ("induced fit"). I will discuss how the temporal ordering of shape changes and binding events can be inferred by modeling data from experiments that probe the binding kinetics, and what we can learn from Markov state modeling of protein binding simulations. Molecular recognition of protein partners anchored in opposing cell membranes depends on the local separation of these membranes. I will present how the coupling between protein binding and membrane separation leads to cooperativity in the stabilization of close-contact zones, e.g. in T cell adhesion and activation.