Building upon the increasingly strong links between physics, chemistry and the life sciences, the program aims at advancing the quantitative and molecular understanding of life processes while at the same time exploring new frontiers of physics. Raising biological research towards a quantitative level requires biophysical research at molecular, cellular, and supracellular levels. At the same time, the increasingly accurate characterization of biomolecules, networks of supramolecular organization, and interacting cellular networks represent complex many-body problems from which new physics emerges.

Research topics include biomolecular structure and dynamics, biological membranes, the underlying cytoskeleton, motor proteins, cell division and intracellular transport, communication and sensory processes, as well as structure and pattern formation in systems of interacting cells and tissues (heart muscle). In bottom up approaches, simplified model systems are generated such as complex fluids (polymers, colloids, membranes, granular materials). These simplified systems require chemical synthesis to understand, control and manipulate molecular processes. Based on such well-defined systems, their dynamics, turbulence and pattern formation can be analyzed. Neuronal information processing, finally, represents the most complex strongly interacting many-particle system.

Theory and numerical simulations are an integral part of many of the experimental projects. Analytical approaches and atomistic or coarse-grained simulations reveal functional details that can be compared to experiments or may even be inaccessible to experiment. A quantitative understanding of phenomena such as protein folding, membrane fusion, cell motility/division, or tissue dynamics, demands new theoretical physics in the areas of non-equilibrium systems, non-linear dynamics, or the dynamics of complex systems.

Nanoresolution far-field microscopy promises unprecedented spatial resolution in fluorescence microscopy. Single-molecule techniques such as optical and atomic force microscopy, address individual biomolecules, e.g. when studying the protein ‘nano-machines’ of the cell. At the atomic level, X-ray crystallography, electron microscopy, NMR and solid state NMR probe biomolecular structure and dynamics. These techniques provide complementary information, not only on the structures of single biomolecules, but also on their interactions which drive the self-organized formation of larger complexes and structures.