Designing Switchable Proteins for Biosensing and Functional Regulation

Abstract: The goal of this work is to convert ordinary proteins into molecular switches whose intrinsic functions can be controlled by binding of molecules of choice. To do so, we employ the strategy of fusing a protein responsible for molecular recognition to a second protein that performs the biological activity of interest. The challenge is to develop general mechanisms by which conformational changes in each domain are transduced to the other to create functional bioswitches. Here, I present our recent progress in creating modular and readily customizable platforms for detecting nucleic acid sequences, small molecules, and proteins. These biosensors employ small, adaptable protein-binding domains, simple DNA devices, and fluorescent and luminescent proteins to achieve specific and sensitive optical readout.

Bio: Stewart Loh received his BS in chemistry from the University of Utah and a PhD in biochemistry from the University of Wisconsin-Madison, where he applied hydrogen exchange NMR methods to investigate folding of staphylococcal nuclease under the guidance of John L. Markley. He continued to study kinetic mechanisms of protein folding as a Damon Runyon-Walter Winchell postdoctoral fellow in the laboratory of Robert L. “Buzz” Baldwin at Stanford University. In 1996, he was appointed Assistant Professor of Biochemistry & Molecular Biology at SUNY Upstate Medical University in Syracuse, NY. He was promoted to Professor in 2008 and has chaired the department since 2024. Dr. Loh was named SUNY Distinguished Professor in 2026.

Zoom Meeting Link: https://utoronto.zoom.us/j/82483832095?pwd=EUWhc4bnR7xuYMUke8NhYcdRT80gt3.1
Zoom Meeting ID: 824 8383 2095
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