The extraordinarily emergent properties of living cells have evolved largely as a consequence of the intricately ordered interactions of their biomolecular components. These cellular building blocks (DNA, RNA, proteins, lipids etc.) interact with one another to form a hierarchy of dynamic, information-rich, macromolecular assemblies that drive a plethora of intriguing biological processes. Unfortunately, despite their central role in cell biology, the requisite structure-functional studies of endogenous multi-subunit macromolecular assemblies still prove to extraordinarily challenging-partially due to their low cellular abundance , dynamic nature, and heterogeneity of these native assemblies. 

    Over the years we have developed enabling integrative structural proteomic technologies to overcome these challenges. We have also applied these new tools to study the architectures and functions of large native macromolecular assemblies that regulate several fundamentally important processes of cell biology including DNA replication, basal gene transcription and its regulations. Most recently, we have begun to unravel the mechanistic details of the eukaryotic nuclear pore complex-the gigantic, ~500 protein machine that has been conserved for over a billion years of evolution, and the sole mediator for nuclear-cytoplasmic transport.

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