MBM Group

Molecular Biomechanics (MBM)

Proteins are exposed to and tightly regulated by external perturbations, binding partners and mechanical stress, altering their assembly and reactivity. Revealing the molecular driving forces and evolutionary constraints in biomolecular systems is a requirement of designing biological materials and processes, for applications in material science and biomedicine, which is the aim of our research. Our research focuses on protein materials and fibers such as silk, disordered proteins and protein folding, the extra-cellular matrix, enzymes and allosteric proteins. Evolutionary design is a complementary aspect we consider for understanding physiological functions of these systems.

The major interest of the Molecular Biomechanics group is to decipher how proteins have been designed to specifically respond to mechanical forces in the cellular environment or as a biomaterial. We use Molecular Dynamics simulations, Force Distribution Analysis, Finite Element Analysis, and other computational techniques to study protein dynamics and mechanics on different length and time scales. More recently, we have combined phylogenomics and computational biophysics to take an evolutionary perspective on the mechanical function of protein. This involves mapping protein structures onto phylogenetic trees to reveal trends in protein folding or mechanical stability. The knowledge thus gleaned provides insights into the differences between present-day proteins and their ancestors a few billion years ago. Our aim is to provide a conclusive answer to the question of how mechanical forces influence living organisms at the level of individual molecules.

The Molecular Biomechanics group, headed by Dr. Frauke Gräter, makes use and further develops various computational and theoretical techniques, among others molecular modelling, high-performance molecular simulations, finite element analysis and bioinformatics approaches. For virtually all of the projects, we extensively collaborate with experimental research labs.

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