Major
Molecular Biology
Anticipated Graduation Year
2025
Access Type
Open Access
Abstract
This study looks at mutant T352V Β-glucosidase B (BglB). The mutant product was hypothesized to show reduced kinetic activity and thermostability compared to the wild-type. This was determined through modeling of the mutation using the FoldIt software. The protein was then purified and expressed through SDS-PAGE and Western Blotting. The results indicate that there was no production of a soluble protein. However, the Western Blot indicates the production of an insoluble protein. FoldIt modeling helps to explain the insoluble protein, as it indicates that the proximity of molecules without binding could cause aggregates to form inclusion bodies.
Faculty Mentors & Instructors
Emma Feeney, PhD, Biology
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Analysis of β-glucosidase Mutant T352V
This study looks at mutant T352V Β-glucosidase B (BglB). The mutant product was hypothesized to show reduced kinetic activity and thermostability compared to the wild-type. This was determined through modeling of the mutation using the FoldIt software. The protein was then purified and expressed through SDS-PAGE and Western Blotting. The results indicate that there was no production of a soluble protein. However, the Western Blot indicates the production of an insoluble protein. FoldIt modeling helps to explain the insoluble protein, as it indicates that the proximity of molecules without binding could cause aggregates to form inclusion bodies.