Florence Tama

It is now well established that large-scale rearrangements in proteins are important for a variety of protein functions including catalysis and regulation of activity. The recent developments in experimental methods, especially cryo-electron microscopy (EM), have revealed that large-molecular assemblies are also highly dynamic. While experiment can provide a tremendous source of information on these dynamical properties, computational methods must be employed to complement experimental observations. The primary motivation behind our studies is to explore using computational approaches, at a near-atomic level, functionally important rearrangements in biological systems observed in experiments at high or low-resolution to obtain new insights into the mechanism of these transformations that are presently inaccessible to experiments.