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Mass Spectrometry Methods for the Study of Glycoproteomics and Sulfoproteomics
Abstract
Characterization of post-translational modifications (PTMs) with mass spectrometry is a rapidly growing field. Advances in mass spectrometry techniques for glycosylation and sulfation are needed due to the biological importance of these PTMs. Glycosylation research yields challenges related to the structural diversity and complexity of the PTM. Sulfation yields other unique challenges related to the lability of the sulfate moiety. This dissertation is divided into two parts related to mass spectrometry analysis and fundamental method development for glycosylation and sulfation. The first three chapters focus on analysis of O-glycopeptides derived from two O-linked glycoproteins. Chapter 1 focuses on the recent advances in glycoproteomics and an overview on techniques associated with characterization of glycoproteins. Chapter 2 investigates the use of Energy-Resolved Collision-Induced Dissociated on non-specific proteolytically digested O-linked glycopeptides. Chapter 3 describes the use of sodium adduction on the fragmentation patterns and dissociation characteristics of O-linked glycopeptides derived with a non-specific protease. The final three chapters are concentrated on advancing analytical techniques for the study of sulfopeptides and discrimination of sulfopeptides and phosphopeptides. Chapter 4 provides an introduction to the challenges associated with investigating the sulfoproteome and the current analytical techniques for characterization of this PTM. Chapter 5 focuses on the stabilization of the sulfate moiety on model sulfopeptides and dissociation characteristics with various sodiated charge carriers. Chapter 6 utilizes ion mobility spectrometry for the discrimination of isobaric sulfopeptides and phosphopeptides with the utilization of group I metal adduction.
Subject Area
Chemistry|Biochemistry
Recommended Citation
Kelly, Maia I, "Mass Spectrometry Methods for the Study of Glycoproteomics and Sulfoproteomics" (2020). ETD collection for University of Nebraska-Lincoln. AAI27956644.
https://digitalcommons.unl.edu/dissertations/AAI27956644