Major
Biology
Anticipated Graduation Year
2024
Access Type
Open Access
Abstract
The overall goal of D2D is to create a dataset that will be used to train artificial intelligence algorithms to model a protein and its function based on its amino acid sequence and/or protein structure (Kleffner et al, 2017.) Having accurate structure/function prediction algorithms is important because it demonstrates specific mutations that affect a protein and aids in theorizing how the location of that mutation will affect its overall function. BglB is a key enzyme component present in cellulase, which completes the final step during cellulose hydrolysis to form glucose, which is used as a source of energy in many organisms (Wright et al, 1992). In this experiment, BglB was mutated at nucleotide 108 from leucine to glutamate in order to observe its effect on catalytic efficiency If BglB is mutated at L108E position, then it will exhibit the same catalytic efficiency in comparison to the wild type because its overall Foldit score suggests high likelihood of expression, and intermolecular modeling analysis also points to normal local interactions. Even though the amino acid would change from being hydrophobic to hydrophilic, it occurs far from the catalytic site, theoretically producing no change to the enzyme’s overall activity (Carlin et al, 2017) .
Faculty Mentors & Instructors
Dr. Emma Feeney, Biochemistry
Supported By
National Science Foundation, Ashley Vater and Justin Seigel Lab at UC-Davis
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Characterizing the BglB L108E Mutation on BglB Protein to Determine Its Effects on Catalytic Efficiency
The overall goal of D2D is to create a dataset that will be used to train artificial intelligence algorithms to model a protein and its function based on its amino acid sequence and/or protein structure (Kleffner et al, 2017.) Having accurate structure/function prediction algorithms is important because it demonstrates specific mutations that affect a protein and aids in theorizing how the location of that mutation will affect its overall function. BglB is a key enzyme component present in cellulase, which completes the final step during cellulose hydrolysis to form glucose, which is used as a source of energy in many organisms (Wright et al, 1992). In this experiment, BglB was mutated at nucleotide 108 from leucine to glutamate in order to observe its effect on catalytic efficiency If BglB is mutated at L108E position, then it will exhibit the same catalytic efficiency in comparison to the wild type because its overall Foldit score suggests high likelihood of expression, and intermolecular modeling analysis also points to normal local interactions. Even though the amino acid would change from being hydrophobic to hydrophilic, it occurs far from the catalytic site, theoretically producing no change to the enzyme’s overall activity (Carlin et al, 2017) .