Presentation Type

Poster

Abstract

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

Available for download on Saturday, October 13, 2018

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Apr 28th, 11:00 AM Apr 28th, 12:00 PM

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