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You searched for +publisher:"Michigan State University" +contributor:("Reid, Gavin E"). Showing records 1 – 2 of 2 total matches.

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Michigan State University

1. Nie, Shuai. Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification.

Degree: 2015, Michigan State University

Thesis Ph. D. Michigan State University. Chemistry 2015.

Advances in the development of mass spectrometry (MS) and tandem mass spectrometry (MS/MS) instrumentation have made this technique a versatile analytical tool to identify, characterize and quantify biomolecules including peptides, proteins, lipids, nucleic acids, oligosaccharides and other metabolites. However, based on the individual physicochemical properties of various biomolecules, biomolecular MS or MS/MS on its own may not necessarily give the desired analytical information. Therefore, chemical labeling strategies which alter the behavior of analytes with respect to their ionization, fragmentation and mass analysis are commonly used to facilitate MS-based analysis of biomolecules. This dissertation focuses on the development of biomolecular chemical labeling strategies for lipids, peptides and proteins, to provide improved capabilities for MS-based qualitative and quantitative analysis. Structural labeling via gas phase ion chemistry provides a convenient and rapid modification method for structural and reactivity characterization of modified biomolecular ions. Here, a novel photo-induced inter-molecular gas-phase cross-linking reaction has been developed to investigate the cross-linking reactivity of individual triacylglyceride (TG) molecules as a function of their structures. Ultraviolet photodissociation tandem mass spectrometry (UVPD-MS/MS) of non-covalent complex ions consisting of TG dimers and protonated diiodoaniline resulted in the formation of multiple cross-linked TG products via homolysis of carbon-iodine bonds, hydrogen abstraction and radical recombination. The efficiency of the UVPD reaction depended on the number of unsaturation sites present within the TG lipids. For MS-based quantification, an approach for the multiplexed relative quantification of aminophospholipids from within two different crude lipid extracts was developed. Relative quantification at the ‘sum composition’ and/or ‘molecular lipid’ levels was achieved using high resolution/accurate mass MS/MS by ratiometric measurement of pairs of ‘reporter’ ions formed via the neutral loss from isobaric stable isotope-labeled d6-‘heavy’ and d6-‘light’ S,S′-dimethylthiobutanoylhydroxysuccinimide and iodine/methanol derivatized aminophospholipid ions. In addition, absolute quantification of full length parathyroid hormone (PTH 1-84), a clinical protein biomarker of secondary hyperparathyroidism, and its in vivo oxidized and truncated variants was achieved using a dual stable isotope-labeled internal standard approach coupled with immunocapture and high resolution LC-MS and MS/MS. Analysis of clinical PTH samples using this strategy revealed that no oxidation or PTH 7-84 occurred in vivo. However, several novel sites of in vivo PTH truncation were discovered. At last, stable isotope-containing dimethyl labeling and multi-dimensional LC-MS/MS were applied for proteomic profiling of human RPMI-8226 cells treated with competitive (i.e., Bortezomib) and non-competitive (i.e., TCH-013)…

Advisors/Committee Members: Reid, Gavin E, Bruening, Merlin L, Tepe, Jetze J, Dantus, Marcos.

Subjects/Keywords: Biomolecules – Analysis; Mass spectrometry; Chemistry; Analytical chemistry; Biochemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Nie, S. (2015). Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification. (Thesis). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:3602

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Nie, Shuai. “Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification.” 2015. Thesis, Michigan State University. Accessed December 13, 2019. http://etd.lib.msu.edu/islandora/object/etd:3602.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Nie, Shuai. “Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification.” 2015. Web. 13 Dec 2019.

Vancouver:

Nie S. Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification. [Internet] [Thesis]. Michigan State University; 2015. [cited 2019 Dec 13]. Available from: http://etd.lib.msu.edu/islandora/object/etd:3602.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Nie S. Chemical labeling strategies for mass spectrometry-based biomolecular identification, characterization and quantification. [Thesis]. Michigan State University; 2015. Available from: http://etd.lib.msu.edu/islandora/object/etd:3602

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Michigan State University

2. Cui, Li. Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis.

Degree: 2014, Michigan State University

Thesis Ph. D. Michigan State University. Chemistry 2014.

Protein post-translational modifications (PTMs), such as phosphorylation, glycosylation, oxidation and methylation, play critical roles in a variety of intra- and intercellular activities, such as cell growth, division, migration and apoptosis. Dysregulation of PTMs may induce various diseases including cancer and diabetes. Mass spectrometry (MS) based proteomics has gained popularity in identifying, characterizing and quantifying proteins with PTMs. Successful structural elucidation of proteins with PTMs largely replies on obtaining fragmentation information from tandem mass spectrometry (MS/MS) of peptides resulting from protein digestion. This dissertation partially focuses on improving the knowledge of phosphopeptide fragmentation chemistry during collision induced dissociation (CID)-MS/MS. Abundant neutral losses of 98 Da are often observed upon ion trap CID-MS/MS of phosphopeptides. Two competing fragmentation pathways are involved in this process, namely the direct loss of H3PO4 and the combined losses of HPO3 and H2O. They produce product ions with different structures but the same m/z values, potentially limiting the utility of CID-MS3 for phosphorylation site localization. Furthermore, phosphate group rearrangement reactions in CID-MS/MS (phosphate groups transfer from one phosphorylated site to another hydroxyl group in the peptide) increase the ambiguity for assigning phosphate groups. In this dissertation, factors influencing the competing fragmentation and phosphate group rearrangement reactions during CID-MS/MS of phosphopeptides have been systematically evaluated using a synthetic phosphopeptide library by varying a number of peptide properties. Both competing fragmentation and phosphate group rearrangement reactions were found to be most problematic for CID-MS/MS of phosphopeptide ions with limited proton mobility. The relative contribution of each competing neutral loss pathway was quantified in a series of regioselective 18O-phosphate ester labeled phosphopeptides by comparing the abundance of the -100 Da (-H3PO318O) versus -98 Da (-(HPO3+H2O)) neutral loss product ions formed upon CID-MS/MS.MS-based methods have also been extensively used for characterization and quantification of proteins containing methionine oxidation. Here parathyroid hormone (PTH), which is responsible for regulation of circulating calcium concentration in plasma, has been analyzed. The oxidation kinetics of PTH was first investigated in vitro with H2O2. The obtained oxidized forms of PTH were characterized by CID-MS/MS. It was found that methionine residues in PTH can mainly be oxidized to sulfoxides. An immuno-LC-MS/MS assay was then successfully developed for simultaneous quantification of native, truncated and oxidized forms of PTH in clinical plasma samples by employing heavy isotope labeled protein and…

Advisors/Committee Members: Reid, Gavin E, Bruening, Merlin L, Borhan, Babak, Weliky, David P.

Subjects/Keywords: Mass spectrometry; Post-translational modification; Fragmentation reactions; Chemistry

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Cui, L. (2014). Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis. (Thesis). Michigan State University. Retrieved from http://etd.lib.msu.edu/islandora/object/etd:2662

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Cui, Li. “Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis.” 2014. Thesis, Michigan State University. Accessed December 13, 2019. http://etd.lib.msu.edu/islandora/object/etd:2662.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Cui, Li. “Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis.” 2014. Web. 13 Dec 2019.

Vancouver:

Cui L. Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis. [Internet] [Thesis]. Michigan State University; 2014. [cited 2019 Dec 13]. Available from: http://etd.lib.msu.edu/islandora/object/etd:2662.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Cui L. Evaluation and improvement of mass spectrometry based strategies for protein post-translational modification analysis. [Thesis]. Michigan State University; 2014. Available from: http://etd.lib.msu.edu/islandora/object/etd:2662

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

.