Biological function on the molecular level is directly related to the 3-dimensional structure of biomolecules, their dynamics and finally their interactions, both with the environment as well as with other biomolecules. Conceptually, the research interests of our laboratory revolve around exploring different faces of this fundamental principle through the use of computational and theoretical methods in close collaboration with experimentalists.

While experimental approaches are making breathtaking steps forward, currently the only way to probe biomolecular structure and dynamics on a single molecule level and with all-atom, femtosecond resolution is through molecular dynamics computer simulations, our primary workhorse.

Specifically, we are interested in intrinsically disordered proteins, which, despite their lack of stable tertiary structure, carry out a multitude of amazing functions in our cells. We strongly believe that these molecules will teach us some completely new principles of how biological systems function on the molecular level.

Also, we are interested in the role of dynamics and entropy (in particular, conformational entropy) in biomolecular processes in general. In many cases, a change in conformational entropy of a protein may be enough to alter its functional state, without any associated conformational change on the level of the average structure.  We are developing new methods both for calculating conformational entropy of biomolecules from computer simulations and for measuring it in the experiment.