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020 ▼a 9780438036000
035 ▼a (MiAaPQ)AAI10748472
035 ▼a (MiAaPQ)upenngdas:13127
040 ▼a MiAaPQ ▼c MiAaPQ ▼d 247004
0820 ▼a 574
1001 ▼a Karch, Kelly R.
24510 ▼a Elucidation of Histone Modifications and Nucleosomal Structure Using Novel Mass Spectrometry Approaches.
260 ▼a [S.l.]: ▼b University of Pennsylvania., ▼c 2018.
260 1 ▼a Ann Arbor: ▼b ProQuest Dissertations & Theses, ▼c 2018.
300 ▼a 183 p.
500 ▼a Source: Dissertation Abstracts International, Volume: 79-10(E), Section: B.
500 ▼a Advisers: Benjamin A. Garcia
5021 ▼a Thesis (Ph.D.)--University of Pennsylvania, 2018.
520 ▼a The fundamental repeating unit of chromatin is the nucleosome, composed of 147 base pairs of DNA wrapped around a histone protein octamer containing two copies of H2A, H2B, H3, and H4. Histone proteins are involved in many critical nuclear proce
520 ▼a Histone function is also mediated through its structure and dynamic properties. Hydrogen-deuterium exchange (HDX) coupled to MS is a powerful technique to monitor these properties in solution. However, traditional HDX-MS studies on histone prote
590 ▼a School code: 0175.
650 4 ▼a Biochemistry.
650 4 ▼a Cellular biology.
650 4 ▼a Analytical chemistry.
690 ▼a 0487
690 ▼a 0379
690 ▼a 0486
71020 ▼a University of Pennsylvania. ▼b Biochemistry and Molecular Biophysics.
7730 ▼t Dissertation Abstracts International ▼g 79-10B(E).
773 ▼t Dissertation Abstract International
790 ▼a 0175
791 ▼a Ph.D.
792 ▼a 2018
793 ▼a English
85640 ▼u http://www.riss.kr/pdu/ddodLink.do?id=T14996989 ▼n KERIS ▼z 이 자료의 원문은 한국교육학술정보원에서 제공합니다.
980 ▼a 201812 ▼f 2019
990 ▼a ***1012033