Major
Neuroscience
Anticipated Graduation Year
2021
Access Type
Open Access
Abstract
Our research explores alternative coding methods for protein primary structures. The motivation is to illuminate structure/function properties that are otherwise obscure using the traditional coding methods. The methodology makes appeal to Gödel-type coding. Critically, it offers up to 20! (≈ 2.418) expressions for a single primary structure. Such numbers vastly exceed those of database archives. To diversify our results, we randomized the amino acid alphabets by placing the overall principle of Gödel’s coding into a program. We focused on the E3 ubiquitin ligase known as MDM2. We specifically used this protein to assess one that is considered a druggable protein.
Faculty Mentors & Instructors
Daniel J. Graham, Dr., Chemistry Department
Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Investigation of Gödel-Type Coding of Protein Primary Structures
Our research explores alternative coding methods for protein primary structures. The motivation is to illuminate structure/function properties that are otherwise obscure using the traditional coding methods. The methodology makes appeal to Gödel-type coding. Critically, it offers up to 20! (≈ 2.418) expressions for a single primary structure. Such numbers vastly exceed those of database archives. To diversify our results, we randomized the amino acid alphabets by placing the overall principle of Gödel’s coding into a program. We focused on the E3 ubiquitin ligase known as MDM2. We specifically used this protein to assess one that is considered a druggable protein.