Naomi Raicu, “Study of Protein Mechanics Using a Novel Force-Clamp Rheometer-Based Protein Hydrogel Software”
Mentor: Ionel Popa, Physics

Protein hydrogels are materials comprised of many proteins that have characteristics of both polymeric hydrogels and proteins, making them both durable and elastic. They allow for determination of mechanical properties of proteins using a bulk approach and may be used as experimental models for proteins that routinely unfold and refold within the human body, such as titin in muscles. Our laboratory has developed a force-clamp (FC) hydrogel rheometer which measures the extension of protein hydrogels, allowing for the observation of protein unfolding through measurements of stress and strain. The purpose of this project is to generate new computer routines and an intuitive graphical user interface for communicating with the FC sensors and a sensitive camera for fluorescence detection, and to control their settings, collect data, generate graphs, and execute other functions as required in our experiments. This computer routine and interface upgrade will allow for the addition of fluorescence drivers to the FC that will measure the fluorescent responses of hydrogels synchronously with the mechanical responses. Measuring the fluorescent response of a hydrogel allows for the observation of protein unfolding patterns, so both stress versus strain measurements and protein unfolding can be synchronously observed for a single hydrogel. Such information can provide insight into the biomechanics of proteins in the human body that will help researchers combat proteopathies, diseases caused by structural abnormalities in proteins that may be accelerated by certain medicinal drugs. Currently, we are investigating the effect of various chemical agents on the strength of Bovine Serum Albumin (BSA) hydrogels, and we will continue this research with the new software to observe the effect that these agents have on protein unfolding. We expect that the chemical agents will have varying effects on protein stability and unfolding patterns.