LDR | | 00000nam u2200205 4500 |
001 | | 000000435558 |
005 | | 20200228101244 |
008 | | 200131s2019 ||||||||||||||||| ||eng d |
020 | |
▼a 9781088315286 |
035 | |
▼a (MiAaPQ)AAI13810152 |
040 | |
▼a MiAaPQ
▼c MiAaPQ
▼d 247004 |
082 | 0 |
▼a 574 |
100 | 1 |
▼a Roy, Raktim. |
245 | 10 |
▼a Structural Studies on the Regulation of Bacterial Translation. |
260 | |
▼a [S.l.]:
▼b Yale University.,
▼c 2019. |
260 | 1 |
▼a Ann Arbor:
▼b ProQuest Dissertations & Theses,
▼c 2019. |
300 | |
▼a 150 p. |
500 | |
▼a Source: Dissertations Abstracts International, Volume: 81-04, Section: B. |
500 | |
▼a Advisor: Steitz, Thomas A. |
502 | 1 |
▼a Thesis (Ph.D.)--Yale University, 2019. |
506 | |
▼a This item must not be sold to any third party vendors. |
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▼a Antimicrobial peptides are derived from a diverse range of species, from lower eukaryotes to humans, with a mechanism of action that often involves binding the bacterial cell membrane and even disrupting the cell wall. Proline-rich antimicrobial peptides (PrAMPs), however do not act on the cell membrane, but are instead actively transported inside bacteria where they bind and inactivate intra-cellular targets. In this thesis I report the crystal structures of Bac71-35, Pyrrhocoricin, Metalnikowin and Oncocin and two of its derivatives bound to the Thermus thermophilus 70S ribosome. Each of those PrAMPs blocks the peptide exit tunnel of the ribosome and interferes with the initiation step of translation |
590 | |
▼a School code: 0265. |
650 | 4 |
▼a Chemistry. |
650 | 4 |
▼a Biophysics. |
650 | 4 |
▼a Biochemistry. |
690 | |
▼a 0485 |
690 | |
▼a 0786 |
690 | |
▼a 0487 |
710 | 20 |
▼a Yale University.
▼b Chemistry. |
773 | 0 |
▼t Dissertations Abstracts International
▼g 81-04B. |
773 | |
▼t Dissertation Abstract International |
790 | |
▼a 0265 |
791 | |
▼a Ph.D. |
792 | |
▼a 2019 |
793 | |
▼a English |
856 | 40 |
▼u http://www.riss.kr/pdu/ddodLink.do?id=T15490636
▼n KERIS
▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다. |
980 | |
▼a 202002
▼f 2020 |
990 | |
▼a ***1008102 |
991 | |
▼a E-BOOK |