Author

FNU Ashima

Graduation Semester and Year

2023

Language

English

Document Type

Thesis

Degree Name

Master of Science in Chemistry

Department

Chemistry and Biochemistry

First Advisor

Saiful M Chowdhury

Abstract

Proteins play important role in carrying out a wide range of cellular activities. They are subjected to various post-translational modifications (PTMs) by the addition of functional groups such as acetyl, phosphoryl, and methyl which leads to changes in their biological functions, localization, activity, and structure. The growth of MS technology has immensely facilitated the identification of PTMs comprehensively. This dissertation focuses on mapping these changes using covalent labeling techniques by tagging carboxylic acid residues, which undergo various kinds of PTMs. The second chapter focuses on the methods designed for Affinity Purification Mass Spectrometry (AP-MS) chemical cross-linking (CXL) of protein complexes. There are numerous methods available for bioconjugation which target cysteine, lysine, and arginine residues. Although carboxyl residues, which are prevalent in proteins, are essential for preserving the protein's functionality, there are currently few accessible selective labeling procedures. We have described a novel reactive probe that allows for the chemoselective modification of acidic residues in peptides and proteins. We evaluated the reactivity of diphenyldiazomethane (DPDAM) in peptides and proteins in the third chapter. The fragmentation patterns of these labeled peptides have been investigated using tandem mass spectrometry.

Keywords

Labeling, Mass spectrometry, Tandem, Post-translational modifications

Disciplines

Chemistry | Physical Sciences and Mathematics

Comments

Degree granted by The University of Texas at Arlington

Available for download on Friday, August 01, 2025

Included in

Chemistry Commons

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