Associate Professor
Department of Physics and Astronomy
Molecular and Cellular Biophyics, University of Denver, CO

"Theoretical polymer physics reveals hidden codes in protein sequences to alter disordered states"

Much of protein science has been devoted to decipher sequence-structure-function relation for folded proteins. In this talk, I will discuss how recent polymer physics based mathematical models can be used to decode sequence-conformation rules in `disordered/undolded' proteins. First, I will highlight the role of the denatured/unfolded state in thermophilic proteins. Thermophilic proteins are foldable proteins that can withstand very high temperatures and are typically extracted from organisms that live at extreme temperatures. Next, we will show our model can be used to describe intrinsically disordered proteins (IDP) revealing many surprises in their behavior. For example, we will show how phosphorylation at specific hot spots can induce drastic conformation changes, even far from modification sites, reminiscing `action at a distance'. Mathematical nature of the formalism provides deep insights to these features, protein evolution and design principles by decoding these simple sequence metrics.

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