Mass spectrometry (MS) has become an important analytical method for proteomic research due to its high mass accuracy, resolution, and
selectivity. Even though the traditional bottom-up MS-based method is still a widespread routine for proteomic analysis, middle- and top-down
approaches should provide more comprehensive characterization of proteins isoforms and post-translational modifications (PTMs) due to their
capabilities of maintaining the connectivity between modifications. The Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometer
equipped with multiple efficient fragmentation techniques offers the ultrahigh mass accuracy and resolution to enable separation and
assignment of overlapped precursor and fragment spectral peaks from extremely complex spectra without ambiguity, which gives us great
advantages in middle- and top-down MS-based proteomic analysis. / A Dissertation submitted to the Department of Chemistry and Biochemistry in partial fulfillment of the
requirements for the degree of Doctor of Philosophy. / Fall Semester 2017. / November 6, 2017. / FT-ICR, LC-MS, Mass spectrometry, Middle-down, Proteomics, Top-down / Includes bibliographical references. / Alan G. Marshall, Professor Directing Dissertation; Hengli Tang, University Representative; John G.
Dorsey, Committee Member; Wei Yang, Committee Member.
| Identifer | oai:union.ndltd.org:fsu.edu/oai:fsu.digital.flvc.org:fsu_605101 |
| Contributors | Jiang, Tingting (author), Marshall, Alan G. (Alan George), 1944- (professor directing dissertation), Tang, Hengli (university representative), Dorsey, John G. (committee member), Yang, Wei (committee member), Florida State University (degree granting institution), College of Arts and Sciences (degree granting college), Department of Chemistry and Biochemistry (degree granting departmentdgg) |
| Publisher | Florida State University |
| Source Sets | Florida State University |
| Language | English, English |
| Detected Language | English |
| Type | Text, text, doctoral thesis |
| Format | 1 online resource (133 pages), computer, application/pdf |
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