| LDR | | 00000nam u2200205 4500 |
| 001 | | 000000432458 |
| 005 | | 20200224130930 |
| 008 | | 200131s2019 ||||||||||||||||| ||eng d |
| 020 | |
▼a 9781088315569 |
| 035 | |
▼a (MiAaPQ)AAI13895514 |
| 040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 247004 |
| 082 | 0 |
▼a 574 |
| 100 | 1 |
▼a Szymczak, Lindsey C. |
| 245 | 10 |
▼a Applications of SAMDI Mass Spectrometry for High-Throughput Reaction Monitoring on Peptide Arrays. |
| 260 | |
▼a [S.l.]:
▼b Northwestern University.,
▼c 2019. |
| 260 | 1 |
▼a Ann Arbor:
▼b ProQuest Dissertations & Theses,
▼c 2019. |
| 300 | |
▼a 202 p. |
| 500 | |
▼a Source: Dissertations Abstracts International, Volume: 81-04, Section: B. |
| 500 | |
▼a Advisor: Mrksich, Milan. |
| 502 | 1 |
▼a Thesis (Ph.D.)--Northwestern University, 2019. |
| 506 | |
▼a This item must not be sold to any third party vendors. |
| 520 | |
▼a This work combines the use of high-throughput mass spectrometry with peptide arrays for to monitor reactions on peptides. The Mrksich lab introduced a high-throughput, label-free, biochemical assay that relies on self-assembled monolayers on gold and matrix-assisted laser desorption/ionization mass spectrometry, termed SAMDI-MS. This dissertation introduces new applications of SAMDI-MS and peptide arrays and illustrates the many advantages of this technique for studying reactions on peptides.Chapter 2 describes the use of SAMDI-MS and peptide arrays for the identification of new sequence-selective reactions of peptides. Selective reactions on peptides and proteins are important for studying protein function and preparing protein-based materials. Using this technique, we discover and characterize the sequence-selective acetylation of peptides containing histidine and tyrosine by acetic anhydride and demonstrate the advantages of using peptide arrays with a label- free analysis method to discover peptide-modifying reactions.We then illustrate the use of SAMDI-MS and phosphorylated peptide arrays to gain a systems- level understanding of phosphatase activity in cell lysates. Phosphorylation is the most prominent post-translational modification on proteins. While phosphorylation plays important roles in many cellular processes, understanding of the regulation of phosphorylation is limited. Kinases and phosphatases work cooperatively to regulate phosphorylation |
| 590 | |
▼a School code: 0163. |
| 650 | 4 |
▼a Chemistry. |
| 650 | 4 |
▼a Biochemistry. |
| 690 | |
▼a 0485 |
| 690 | |
▼a 0487 |
| 710 | 20 |
▼a Northwestern University.
▼b Chemistry. |
| 773 | 0 |
▼t Dissertations Abstracts International
▼g 81-04B. |
| 773 | |
▼t Dissertation Abstract International |
| 790 | |
▼a 0163 |
| 791 | |
▼a Ph.D. |
| 792 | |
▼a 2019 |
| 793 | |
▼a English |
| 856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T15491614
▼n KERIS
▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |
| 980 | |
▼a 202002
▼f 2020 |
| 990 | |
▼a ***1008102 |
| 991 | |
▼a E-BOOK |