Large protein complexes carry out some of the most complex functions in biology. Such structures are often assembled spontaneously from individual components through the process of self-assembly. A fundamental challenge in biology is to understand how protein subunits have evolved the remarkable ability to spontaneously self-assembly into complex structures and to characterize the interactions, assembly pathway and three-dimensional structures of such protein assemblies. The concept of self-assembly is relevant not only in the study of naturally occurring systems, but as a design principle in the engineering of novel protein assemblies.
We combine computational and experimental methods to understand protein assembly formation. Computational methods are developed to predict the 3D structure of protein assemblies at high resolution. Computational protein design is used to rationally design novel protein assemblies which are then characterized using experimental methods.
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