Gabriel Wright, Ph.D.

Assistant Professor

  • Milwaukee WI UNITED STATES
  • Diercks Hall DH414
  • Computer Science

Gabriel Wright's primary research work is in computational biology.

Contact

Education, Licensure and Certification

Ph.D.

Computer Science and Engineering

University of Notre Dame

2021

M.S.

Computer Science and Engineering

University of Notre Dame

2020

B.A.

Mathematics

Concordia College

2016

Biography

Gabriel Wright is an Assistant Professor of Computer Science at the Milwaukee School of Engineering. He graduated with a Ph.D. in Computer Science and Engineering from the University of Notre Dame in May, 2021. Gabriel’s primary research work is in computational biology, specifically studying the effects of rare codons on resulting protein expression, folding, and function.

Areas of Expertise

Co-translational Protein Folding
Computational Biology
Synonymous Codon Usage

Accomplishments

Arthur J. Schmitt Leadership Fellowship

University of Notre Dame, 2016 – 2021

Event and Speaking Appearances

A New Look at Codon Usage and Protein Expression

11th International Conference on Bioinformatics and Computational Biology  

Analysis of Popular Computational Codon Usage Models and Their Association With Ribosome Footprinting Implied Translational Slowdowns

Great Lakes Bioinformatics Conference  

HarMinMax: Harmonizing Codon Usage to Replicate Local Host Trans- lation

ACM International Conference on Bioinformatics, Computational Biology, and Health Informatics  

Selected Publications

CHARMING: Harmonizing synonymous codon usage to replicate a desired codon usage pattern

Protein Science

There is a growing appreciation that synonymous codon usage, although historically regarded as phenotypically silent, can instead alter a wide range of mechanisms related to functional protein production, a term we use here to describe the net effect of transcription (mRNA synthesis), mRNA half-life, translation (protein synthesis) and the probability of a protein folding correctly to its active, functional structure. In particular, recent discoveries have highlighted the important role that sub-optimal codons can play in modifying co-translational protein folding. These results have drawn increased attention to the patterns of synonymous codon usage within coding sequences, particularly in light of the discovery that these patterns can be conserved across evolution for homologous proteins. Because synonymous codon usage differs between organisms, for heterologous gene expression it can be desirable to make synonymous codon substitutions to match the codon usage pattern from the original organism in the heterologous expression host. Here we present CHARMING (for Codon HARMonizING), a robust and versatile algorithm to design mRNA sequences for heterologous gene expression and other related codon harmonization tasks. CHARMING can be run as a downloadable Python script or via a web portal at http://www.codons.org.

Network analysis of synonymous codon usage

Bioinformatics

Most amino acids are encoded by multiple synonymous codons, some of which are used more rarely than others. Analyses of positions of such rare codons in protein sequences revealed that rare codons can impact co-translational protein folding and that positions of some rare codons are evolutionarily conserved.

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Analysis of computational codon usage models and their association with translationally slow codons

PloS one

Improved computational modeling of protein translation rates, including better prediction of where translational slowdowns along an mRNA sequence may occur, is critical for understanding co-translational folding. Because codons within a synonymous codon group are translated at different rates, many computational translation models rely on analyzing synonymous codons. Some models rely on genome-wide codon usage bias (CUB), believing that globally rare and common codons are the most informative of slow and fast translation, respectively.

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