Bioengineering Seminar Series
Tuning Protein Structure by Changing Solution Conditions
Dept. of Chemistry and Chemical Biology, UC Merced
Friday, October 25, 2019
10:30 AM in COB 110
For decades, protein function has been understood in the context of their three-dimensional structure. More recently, a new class of intrinsically disordered proteins (IDPs) has upended this convention. Unlike well-folded proteins, IDP activity is determined by structural preferences in an ensemble of rapidly interchanging conformations that can strongly depend on solution conditions. We use a multi-scale approach to measure IDP structural changes in silico, in the test tube, and in live cells. Our experiments reveal that IDPs can possess a highly tunable structural ensemble that depends on the chemical composition of their environment as much as it does on protein sequence.
Shahar Sukenik opened his lab at UC Merced in August 2018. The lab combines simulation, biophysical, and microscopy methods to study the interactions between proteins and their surrounding environments, in the test tube and in the cell. He obtained his PhD at the Hebrew University of Jerusalem, Israel, and did his postdoc at the University of Illinois at Urbana-Champaign.
For additional information contact Professor Victor Muñoz