Emmanuel Levy, PhD, investigates the principles of protein assembly and self-organization in the proteome. The proteome is the entire set of proteins that can be expressed at a given time, and even for a simple organism like baker’s yeast—the model organism he studies in his laboratory—the proteome involves a choreography between tens of millions of proteins. The task of understanding how these millions of proteins assemble and work together to support life is extraordinarily complex. Levy is taking an interdisciplinary approach to address this challenge and has revealed basic principles of this choreography, at multiple scales. At the most fundamental level, protein assembly takes place by homo-oligomerization, in which identical copies of a protein become arranged symmetrically into higher-order structures that can possess functionality. These so-called quaternary structures can be predicted using a computational strategy that Levy devised for many thousands of proteins of known structure. Zooming-out one level, he predicted and demonstrated experimentally that symmetric homo-oligomers are highly susceptible to forming infinitely long polymers by mutation. These findings shift the paradigm of how quickly new protein assemblies can emerge during evolution. Zooming out yet another level, Levy developed effective methods for the systematic tagging of proteins in yeast cells and their visualization. Levy’s research, which bridges atomic and cellular scales, generates original concepts and powerful tools for probing and grasping the molecular “sociology” of proteins inside living cells.
For details of his research and recent publication, please visit HERE.
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