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Articles 1 - 9 of 9
Full-Text Articles in Life Sciences
High Resolution Mass Spectrometry As A Platform For The Analysis Of Polyoxometalates, Their Solution Phase Dynamics, And Their Biological Interactions., Daniel T. Favre
High Resolution Mass Spectrometry As A Platform For The Analysis Of Polyoxometalates, Their Solution Phase Dynamics, And Their Biological Interactions., Daniel T. Favre
Doctoral Dissertations
Polyoxometalates (POMs) are a class of inorganic molecule of increasing interest to the inorganic, bioinorganic and catalytic communities among many others. While their prevalence in research has increased, tools and methodologies for the analysis of their fundamental characteristics still need further development. Decavanadate (V10) specifically has been postulated to have several unique properties that have not been confirmed independently. Mass spectrometry (MS) and its ability to determine the composition of solution phase species by both mass and charge is uniquely well suited to the analysis of POMs. In this work we utilized high-resolution mass spectrometry to characterize V10 in aqueous …
Deciphering Protein Higher-Order Structure And Interactions Via Diethylpyrocarbonate Labeling-Mass Spectrometry, Xiao Pan
Doctoral Dissertations
The study of protein higher-order structures is vital because it is closely related to the investigation of protein folding, aggregation, interaction and protein therapeutics. Consequently, numerous biochemical and biophysical tools have been developed to study protein higher-order structures in many different situations. The combination of covalent labeling (CL) and mass spectrometry (MS) has emerged as a powerful tool for studying protein structures and offers many advantages over other traditional techniques, such as better structural coverage, high throughput, high sensitivity, and the ability to study proteins in mixtures. This dissertation focuses on diethylpyrocarbonate (DEPC) as an effective CL reagent that can …
Amyloidogenesis Of Β-2-Microglobulin Studied By Mass Spectrometry And Covalent Labeling, Blaise G. Arden
Amyloidogenesis Of Β-2-Microglobulin Studied By Mass Spectrometry And Covalent Labeling, Blaise G. Arden
Doctoral Dissertations
Amyloid-forming proteins are implicated in a number of debilitating diseases. While many amyloid-forming proteins are well studied, the early stages of amyloidosis are still not well understood on a molecular level. Covalent labeling, combined with mass spectrometry (CL-MS), is uniquely well suited to provide molecular-level insight into the factors governing the early stages of amyloidosis. This dissertation leverages CL-MS techniques to examine the early stages of β-2-microglobulin (β2m) amyloidosis. β2m is the protein that forms amyloids in the condition known as dialysis-related amyloidosis. An automated CL-MS technique that uses dimethyl(2-hydroxy-5-nitrobenzyl) sulfonium bromide as a labeling reagent was developed and used …
Structural Analysis Of Protein Therapeutics By Hydrogen Deuterium Exchange And Covalent Labeling Mass Spectrometry, Catherine Yvonne Tremblay
Structural Analysis Of Protein Therapeutics By Hydrogen Deuterium Exchange And Covalent Labeling Mass Spectrometry, Catherine Yvonne Tremblay
Doctoral Dissertations
This dissertation focuses on the use of mass spectrometry (MS) to study therapeutic protein higher order structure (HOS) by encoding the structure into the mass of the protein. As therapeutic proteins become more common in the pharmaceutical industry, the need for methods that accurately determine their HOS has grown. Two methods applied here are hydrogen deuterium exchange (HDX) MS and diethylpyrocarbonate (DEPC) covalent labeling (CL) MS. We demonstrate how these two methods provide complementary, and sometimes synergistic, information about protein HOS. HDX/MS reports on both changes in solvent exposure and changes in protein dynamics, and as a result it can …
Structural Analysis Of Protein Therapeutics Using Covalent Labeling – Mass Spectrometry, Patanachai Limpikirati
Structural Analysis Of Protein Therapeutics Using Covalent Labeling – Mass Spectrometry, Patanachai Limpikirati
Doctoral Dissertations
Using mass spectrometry (MS) to obtain information about a higher order structure of protein requires that a protein’s structural properties are encoded into the mass of that protein. Covalent labeling (CL) with reagents that can irreversibly modify solvent accessible amino acid side chains is an effective way to encode structural information into the mass of a protein, as this information can be read-out in a straightforward manner using standard MS-based proteomics techniques. The differential reactivity of proteins under two or more conditions can be used to distinguish protein topologies, conformations, and/or binding sites. CL-MS methods have been effectively used for …
Covalent Labeling-Mass Spectrometry For Characterizing Protein-Ligand Complexes, Tianying Liu
Covalent Labeling-Mass Spectrometry For Characterizing Protein-Ligand Complexes, Tianying Liu
Doctoral Dissertations
This dissertation focuses on applying covalent labeling (CL) and mass spectrometry (MS) for characterizing protein-ligand complexes. Understanding protein-ligand interactions has both fundamental and applied significance. Covalent labeling is a protein surface modification technique that selectively modifies solvent-exposed amino acid side chains of proteins. A covalent bond is formed between the functional groups of labeling reagent and protein’s side chain. One of the key factors that affects CL reactivity is a side chain’s solvent accessibility. Ligand binding protects residues on the protein surface from being labeled, and residues involved in ligand binding can be indicated via decreases in labeling extents. The …
The Application Of Hydrogen/Deuterium Exchange And Covalent Labeling Coupled With Mass Spectrometry To Examine Protein Structure, Nicholas B. Borotto
The Application Of Hydrogen/Deuterium Exchange And Covalent Labeling Coupled With Mass Spectrometry To Examine Protein Structure, Nicholas B. Borotto
Doctoral Dissertations
Thorough insight into a protein’s structure is necessary to understand how it functions and what goes wrong when it malfunctions. The structure of proteins, however, is not easily analyzed. The analysis must take place under a narrow range of conditions or risk perturbing the very structure being probed. Furthermore, the wide diversity in size and chemistry possible in proteins significantly complicates this analysis. Despite this numerous methods have been developed in order to analyze protein structure. In this work, we demonstrate that mass spectrometry (MS)-based techniques are capable of characterizing the structure of particularly challenging proteins. This is done through …
Studying Nanoparticle/Cell And Nanoparticle/Biosurface Interaction With Mass Spectrometry, Singyuk Hou
Studying Nanoparticle/Cell And Nanoparticle/Biosurface Interaction With Mass Spectrometry, Singyuk Hou
Masters Theses
Nanoparticles (NPs) have been used widely in various fields ranging from biomedical applications to life science due to their highly tunable properties. It is essential to understanding how NPs interact with biological systems of interest, therefore, analytical platforms to efficiently track NPs from cell to animal level are essential. In this thesis, laser desorption ionization mass spectrometry (LDI-MS) and inductively-coupled plasma mass spectrometry (ICP-MS) has been developed and applied to quantify NP/cell and NP/biological surface interactions. These two methods provide fast, label-free and quantitative analysis. New capability of LDI-MS to differentiate cell surface-bound and internalized NPs were established and ICP-MS …
Characterization Of Protein-Protein Interactions For Therapeutic Drug Design Utilizing Mass Spectrometry, Alex J. Johnson
Characterization Of Protein-Protein Interactions For Therapeutic Drug Design Utilizing Mass Spectrometry, Alex J. Johnson
Masters Theses
The number of transferrin based therapeutics progressing to clinical trials remains disappointingly small despite promising capabilities of transporting therapeutic payloads to cancer cells and across the blood brain barrier. This meager success record is largely due to the complexity and heterogeneity of all protein conjugation products that generates difficulties for their analytical characterization. Discussed in this work, transferrin is conjugated to lysozyme as a model therapeutic to deliver this bacteriostatic protein to target central nervous system infections. In this work ESI- and MALDI-MS were used to characterize the modification sites at lysine residues in hopes of characterizing heterogeneity within the …