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

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

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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.