Presentation Title
Major
Forensic Science
Anticipated Graduation Year
2023
Access Type
Open Access
Abstract
The purpose of this experiment was to characterize the functionality of BglB mutants and generate datasets to train artificial intelligence algorithms to predict mutant functionality. It was hypothesized that mutant Y118F would demonstrate decreased catalytic efficiency and thermostability compared to WT based on the predictive capacities of Foldit, a predictive modeling software. Foldit predicted decreased local interactions such as hydrogen bonds for mutant Y118F, suggesting decreased stability. Experimentation was performed to analyze the enzymatic activity and thermostability of mutant Y118F.
Faculty Mentors & Instructors
Emma Feeney, Ph.D. Molecular Biology
Supported By
Ashley Vater, Justin Siegel Lab at UC-Davis, National Science Foundation.
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Characterizing the Enzymatic Activity and Thermostability of Protein β-Glucosidase B (BglB) Mutant Y118F
The purpose of this experiment was to characterize the functionality of BglB mutants and generate datasets to train artificial intelligence algorithms to predict mutant functionality. It was hypothesized that mutant Y118F would demonstrate decreased catalytic efficiency and thermostability compared to WT based on the predictive capacities of Foldit, a predictive modeling software. Foldit predicted decreased local interactions such as hydrogen bonds for mutant Y118F, suggesting decreased stability. Experimentation was performed to analyze the enzymatic activity and thermostability of mutant Y118F.