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Single-Molecule Investigation of Multi-Domain Folding: A Fluorescence Correlation Spectroscopy Study

Faculty Mentor: Michelle Bunagan

Students: Andrew Apicello & Priya Gupta

The focus of our project is on human serum albumin (HSA), which is a protein that can bind to many ligands (ions or molecules that form a certain type of bond with the molecule in question) and is therefore important in the study of interactions between proteins and drugs. The goal is to determine the important intermediate conformations that are accessed by HSA during the folding and unfolding process and thereby determine the specific folding pathway and folding energy landscape.  To accomplish this, FCS (fluorescence correlation spectroscopy) will be used to measure the radius of single protein molecules.  These experiments will be done in various concentrations of chemical denaturants, such as urea and guanidine hydrochloride, which will cause the protein to unfold and likely access these intermediate states.  Dyes (like Alexa Fluor 488) will be used to label domains on the protein so that it may be detected by the FCS equipment.