| LDR | | 00000nam u2200205 4500 |
| 001 | | 000000435827 |
| 005 | | 20200228105821 |
| 008 | | 200131s2018 ||||||||||||||||| ||eng d |
| 020 | |
▼a 9781085557153 |
| 035 | |
▼a (MiAaPQ)AAI10930539 |
| 040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 247004 |
| 082 | 0 |
▼a 540 |
| 100 | 1 |
▼a Riley, Nicholas M. |
| 245 | 10 |
▼a Advancing Electron Transfer Dissociation Technologies for Characterization of Proteomes and Post-translational Modifications. |
| 260 | |
▼a [S.l.]:
▼b The University of Wisconsin - Madison.,
▼c 2018. |
| 260 | 1 |
▼a Ann Arbor:
▼b ProQuest Dissertations & Theses,
▼c 2018. |
| 300 | |
▼a 440 p. |
| 500 | |
▼a Source: Dissertations Abstracts International, Volume: 81-02, Section: B. |
| 500 | |
▼a Advisor: Coon, Joshua J. |
| 502 | 1 |
▼a Thesis (Ph.D.)--The University of Wisconsin - Madison, 2018. |
| 506 | |
▼a This item must not be sold to any third party vendors. |
| 520 | |
▼a This dissertation presents research focusing on the development of new instrumentation and methodology to leverage ion-ion reactions for proteomic analyses. Electron transfer dissociation (ETD) technologies have proven a valuable alternative to collision-based fragmentation methods for sequencing peptides and proteins to advance global proteome characterization. Chapter 1 outlines the core concepts central to mass spectrometry (MS)-based proteomics, in addition to the basic principles of ETD and various strategies to improve its efficacy-including the technology that is the focus of this work, i.e., activated ion ETD (AI-ETD). Chapter 2 describes the first application of AI-ETD to intact proteins, which are more chemically complex and, thus, more difficult to sequence, than their peptide counterparts. Chapter 3 discusses a new strategy to improve signal to-noise in ETD spectra, which is especially beneficial for intact protein analysis and which has been incorporated into the newest generation of commercially available quadrupole-Orbitrap-linear ion trap hybrid MS systems. AI-ETD capabilities were also recently implemented on this state-of-the-art MS system (Chapter 4), and the ability to perform AI-ETD on this instrument enables comprehensive sequence coverage of moderately-sized intact proteins (Chapter 5), significantly improves proteoform characterization in large-scale analyses of complex mixtures of intact proteins (Chapter 6), and also enhances characterization of larger intact proteins (Chapter 7). Furthermore, AI-ETD improves characterization of post-translational modifications. Chapter 8 demonstrates the utility of AI-ETD for phosphosite localization in phosphopeptides and intact phosphoproteins, and Chapter 9 presents the largest glycoproteomic study to date by using AI-ETD to interrogate intact N-glycopeptides. Beyond positive-mode analyses of peptide and protein cations, ion-ion reactions also bring unique benefits to negative-mode analyses of precursor anions, where collision-based dissociation fails to consistently produce sequence-informative fragments. Chapter 10 describes implementation of negative ETD (NETD) and activated ion NETD (AI-NETD) and their application to whole-proteome sequencing in the negative mode, and Chapter 11 presents a modified search algorithm to improve interpretation of large-scale NETD and AI-NETD data. Conclusions and future directions of these projects are discussed in Chapter 12. |
| 590 | |
▼a School code: 0262. |
| 650 | 4 |
▼a Analytical chemistry. |
| 650 | 4 |
▼a Chemistry. |
| 690 | |
▼a 0486 |
| 690 | |
▼a 0485 |
| 710 | 20 |
▼a The University of Wisconsin - Madison.
▼b Chemistry. |
| 773 | 0 |
▼t Dissertations Abstracts International
▼g 81-02B. |
| 773 | |
▼t Dissertation Abstract International |
| 790 | |
▼a 0262 |
| 791 | |
▼a Ph.D. |
| 792 | |
▼a 2018 |
| 793 | |
▼a English |
| 856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T15490351
▼n KERIS
▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |
| 980 | |
▼a 202002
▼f 2020 |
| 990 | |
▼a ***1008102 |
| 991 | |
▼a E-BOOK |