I investigate how structure and dynamics of proteins interplay with their biological function. Currently, I study the structure/dynamics properties of cytoskeleton-regulating proteins which consist of multiple structured domains (modules). Many of such modular proteins are capable of altering their roles in response to cell signals by repositioning the domains relatively to each other while each individual domain remains structurally unperturbed. Multi-domain proteins constitute the majority of human proteome yet their very flexibility and capacity to rearrange often prevent their structural characterization by most techniques (e.g. x-ray crystallography). Methods I specialize in (especially Nuclear Magnetic Resonance spectroscopy or NMR) combined with general biochemical approaches deliver site-specific information about the structure, dynamics and function of modular proteins. I am especially interested in deciphering the roles of the inter-domain linkers by understanding how their length, residue composition and backbone dynamics relate to the function of the corresponding modular proteins.
