Start Date
17-4-2024 2:15 PM
Location
2nd floor - Library
Abstract
Foldit Standalone software is a program that allows for structural manipulation of proteins. It can be used to observe the 3-dimensional structure of proteins, calculating the relative stability of the protein. Mutations can be made to the structure of the protein on Foldit, which can then have stability values calculated as well. Foldit can be used to minimize energy values of proteins, measuring changes in energy due to mutations and in the end providing a Foldit energy value. In our work, we seek to use Foldit to calculate energy values of a mutated protein, then compare these values to those calculated in experiment, overall establishing a basis for comparison of the Foldit energy values. We observed Cytochrome C (Cyt c) , a small heme protein that functions in the electron transport chain. Previously done work observed the protein unfolding of Cyt c, then spectroscopically analyzed the protein through fluorescence, absorbance, and circular dichroism, allowing for calculations of Gibbs free energy of specific mutations to be made. Using Foldit, we were able to view these mutations, observing their effects on energy values and protein stability. In comparing the energy values calculated from Foldit with those spectroscopically measured, we can understand the degree of accuracy that Foldit predicts protein stability with. We were particularly interested in observing Cyt c because Foldit ignores prosthetic groups, meaning it does not consider heme groups. This fact made us particularly interested in seeing how Foldit energy values would compare to experimental energy values.
Comparison of Foldit Calculated Stability with Experimentally Determined Energy Values of Cytochrome C Mutants
2nd floor - Library
Foldit Standalone software is a program that allows for structural manipulation of proteins. It can be used to observe the 3-dimensional structure of proteins, calculating the relative stability of the protein. Mutations can be made to the structure of the protein on Foldit, which can then have stability values calculated as well. Foldit can be used to minimize energy values of proteins, measuring changes in energy due to mutations and in the end providing a Foldit energy value. In our work, we seek to use Foldit to calculate energy values of a mutated protein, then compare these values to those calculated in experiment, overall establishing a basis for comparison of the Foldit energy values. We observed Cytochrome C (Cyt c) , a small heme protein that functions in the electron transport chain. Previously done work observed the protein unfolding of Cyt c, then spectroscopically analyzed the protein through fluorescence, absorbance, and circular dichroism, allowing for calculations of Gibbs free energy of specific mutations to be made. Using Foldit, we were able to view these mutations, observing their effects on energy values and protein stability. In comparing the energy values calculated from Foldit with those spectroscopically measured, we can understand the degree of accuracy that Foldit predicts protein stability with. We were particularly interested in observing Cyt c because Foldit ignores prosthetic groups, meaning it does not consider heme groups. This fact made us particularly interested in seeing how Foldit energy values would compare to experimental energy values.
