Major
Forensic Science
Anticipated Graduation Year
Seniors
Access Type
Open Access
Abstract
The purpose of this research was to analyze the difference between β-glucosidase B (BglB) wild-type enzyme and BglB-Histidine-328-Asparagine (H328N). We hypothesized that this mutation will demonstrate decreased catalytic efficiency and thermostability in comparison to the wild-type because of a change in Rosetta scores, shown by an overall energy increase. We based our assumption off of the results we obtained from the Foldit, a mutation simulation program. Further testing through enzymatic and thermostability assays will give us more information on the mutation.
Community Partners
Ashley Vater at Justin Siegel Lab at UC-Davis
Faculty Mentors & Instructors
Dr. Emma Feeney
Supported By
National Science Foundation
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Characterization of Enzymatic Activity and Thermostability of Beta-Glucosidase B (BglB)-Histidine-328-Asparagine for D2D Database Contribution
The purpose of this research was to analyze the difference between β-glucosidase B (BglB) wild-type enzyme and BglB-Histidine-328-Asparagine (H328N). We hypothesized that this mutation will demonstrate decreased catalytic efficiency and thermostability in comparison to the wild-type because of a change in Rosetta scores, shown by an overall energy increase. We based our assumption off of the results we obtained from the Foldit, a mutation simulation program. Further testing through enzymatic and thermostability assays will give us more information on the mutation.