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Our research group focuses and experts at studying macromolecular assemblies in realistic solution conditions. The structures were are investigating are often too dynamic, too soft, or too large in molecular weight to be crystalized and in some cases too thick or dense for electron microscopy. The molecular subunits of the large assemblies are often too small for optical microscopy. Hence, in many cases, the challenges of structural biophysics were inaccessible. Our lab is developing pioneering solution X-ray scattering-based technology to address and resolve these challenges.
We are developing state-of-the-art measurements and analysis capabilities that enable us to study self-assembled biomolecules in solutions. By applying state-of-the-art data analysis, integrated with simulations, theory, and various algorithms (maximum entropy optimization, for example), we have been resolving the structures and intermolecular interactions in complex, weakly ordered, and dynamic self-assembling biological structures. Our research spans virus self-assembly, the assembly of cytoskeletal filamentous proteins and their associated proteins, and lipid membranes.
Studying relatively simple model systems, where fundamental physical chemistry questions can be addressed in great detail is essential for understanding complex biological structures. Our goal is to use, develop, and improve analysis tools towards high-resolution complex structures as well as for time-resolved measurements of various biomolecular dynamic architectures. Our challenges are to address assembled structures that can attain equilibrium as well as dissipative self-assembled structures that operate out-of-equilibrium owing to a constant supply of chemical energy. This mode of assembly is ubiquitous in nature but is poorly understood. This knowledge has biomedical implications in drug design and is required for developing novel biomaterials, advanced drug-delivery formulations, nanoreactors, and for displaying antigens for vaccine applications.
