Major
Forensic Science
Anticipated Graduation Year
2023
Access Type
Open Access
Abstract
The purpose of this project is to contribute data to the Design to Data (D2D) database, which aims create software to predict protein functionality. We will be analyzing our mutant enzyme through a series of experiments that will look at the enzymatic activity and thermostability in comparison to the wild type enzyme. We hypothesize that B-glucosidase (BglB) mutant H178C will demonstrate decreased catalytic efficiency and thermal stability in comparison to the wild type because its overall Foldit score suggests a lower likelihood of expression, despite having minimal effect on local hydrogen bonds and hydrophobic interactions.
Community Partners
Ashley Vater, Justin Siegel Lab - UC Davis
Faculty Mentors & Instructors
Emma Feeney, PhD, Biochemistry
Supported By
National Science Foundation
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Analysis of the H178C Mutation on β-glucosidase (BglB) Protein
The purpose of this project is to contribute data to the Design to Data (D2D) database, which aims create software to predict protein functionality. We will be analyzing our mutant enzyme through a series of experiments that will look at the enzymatic activity and thermostability in comparison to the wild type enzyme. We hypothesize that B-glucosidase (BglB) mutant H178C will demonstrate decreased catalytic efficiency and thermal stability in comparison to the wild type because its overall Foldit score suggests a lower likelihood of expression, despite having minimal effect on local hydrogen bonds and hydrophobic interactions.