NEW METHODS TO QUANTIFY METHIONINE OXIDATION AND PROTEIN GLYCOSYLATION AND A DE NOVO GLYCOPEPTIDE DECOY GENERATOR

Protein post-translational modifications (PTMs) produce complex, heterogeneous species that can best be identified and analyzed using mass spectrometry (MS). The ever-growing number of protein bioetherapeutics need effective MS tools to characterize PTMs and ensure drug safety and efficacy. Methionine oxidation and glycosylation are two PTMs that can impact protein structure, stability and pharmokinetic properties. The highly spontaneous nature of methionine oxidation makes it challenging to analyze because biologically irrelevant oxidation can be introduced during sample preparation that is indiscriminable from oxidation that impacts protein function. Chapter Two of this dissertation applies a sample preparation strategy that elucidates how much oxidation is present in native protein samples to HIV-1 Env by developing a new data analysis strategy that can be applied to the multiple-methionine containing peptides found in the tryptic digests of the protein.

Name thesis:degree_name

Ph.D.

Discipline thesis:degree_discipline

Chemistry

Grantor dc:publisher

University of Kansas

Year dc:date.issued

2019

Author dc:creator

• SHIPMAN, JOSHUA Thomas

Advisor dc:contributor.advisor

• Desaire, Heather

Language dc:language.iso

en

Dc Identifier Other

https://www.proquest.com/LegacyDocView/DISSNUM/27543294

OAI identifier oai:identifier

oai:kuscholarworks.ku.edu:1808/37176