Event Title
Secondary Protein Structure Analysis of Cu, Zn Superoxide Dismutase Aggregates Found in ALS
Co-investigators
Megan Bourassa (Stony Brook University); Joan S. Valentine (University of California); David R. Borchelt (University of Florida); Lisa Miller (Brookhaven National Laboratory)
Faculty Mentor
Ashok Puri
Location
Memorial Gym
Start Date
20-4-2012 2:30 PM
End Date
20-4-2012 3:30 PM
Description
This study seeks to compare the secondary structure of the protein aggregates in four common mutations of Cu/Zn Superoxide Dismutase (SOD1) in order to understand how SOD1 mutant protein aggregates cause motor neuron cell apoptosis. Chinese hamster ovary (CHO) cells were grown on silicon nitride windows and transfected to express SOD1 mutations (A4V, H80R, D125H, G37R, wild type, and non-transgenic controls) co-expressed with yellow fluorescent protein. CHO cells were later subjected to transmission mode Fourier transform infrared spectroscopy from which amide I peaks was analyzed for protein secondary structures. Different transfection time rates with different degrees of aggregation were discovered among the mutations.
Secondary Protein Structure Analysis of Cu, Zn Superoxide Dismutase Aggregates Found in ALS
Memorial Gym
This study seeks to compare the secondary structure of the protein aggregates in four common mutations of Cu/Zn Superoxide Dismutase (SOD1) in order to understand how SOD1 mutant protein aggregates cause motor neuron cell apoptosis. Chinese hamster ovary (CHO) cells were grown on silicon nitride windows and transfected to express SOD1 mutations (A4V, H80R, D125H, G37R, wild type, and non-transgenic controls) co-expressed with yellow fluorescent protein. CHO cells were later subjected to transmission mode Fourier transform infrared spectroscopy from which amide I peaks was analyzed for protein secondary structures. Different transfection time rates with different degrees of aggregation were discovered among the mutations.
Comments
Poster presentation