Poster Session #1: UC South Ballroom
Using Fluorescence Correlation Spectroscopy to Measure Partial Unfolding of Variants of Cytochrome c
Presentation Type
Poster
Faculty Mentor’s Full Name
Bruce Bowler
Faculty Mentor’s Department
Department of Chemistry & Biochemistry and Center for Biomolecular Structure & Dynamics
Abstract / Artist's Statement
The protein Cytochrome c (Cytc) has been known to be a regulatory on/off switch for apoptosis, or programmed cell death, when unfolded. Using Guanidine Hydrochloride (GuHCl) of different concentrations to denature 3 variants of Zinc Cytc (ZnCytc), the unfolding of this protein can be measured. Measuring is performed through different methods such as single- and dual-focus Fluorescence Correlation Spectroscopy (FCS) and Circular Dichroism (CD). FCS is used to measure the change in lifetime of the protein to determine if the protein has unfolded. The change in lifetime is a characterization of partially unfolded proteins. Data are recorded and analyzed through several different Matlab codes to fully understand the folding code of the protein
Category
Physical Sciences
Using Fluorescence Correlation Spectroscopy to Measure Partial Unfolding of Variants of Cytochrome c
UC South Ballroom
The protein Cytochrome c (Cytc) has been known to be a regulatory on/off switch for apoptosis, or programmed cell death, when unfolded. Using Guanidine Hydrochloride (GuHCl) of different concentrations to denature 3 variants of Zinc Cytc (ZnCytc), the unfolding of this protein can be measured. Measuring is performed through different methods such as single- and dual-focus Fluorescence Correlation Spectroscopy (FCS) and Circular Dichroism (CD). FCS is used to measure the change in lifetime of the protein to determine if the protein has unfolded. The change in lifetime is a characterization of partially unfolded proteins. Data are recorded and analyzed through several different Matlab codes to fully understand the folding code of the protein