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Characterization of Protein Sequence Variants and Posttranlational Modifications by Top-down Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Title: Characterization of Protein Sequence Variants and Posttranlational Modifications by Top-down Fourier Transform Ion Cyclotron Resonance Mass Spectrometry.
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Name(s): Dang, Xibei, author
Marshall, Alan G. (Alan George), 1944-, professor directing dissertation
Gilbert, David M., university representative
Roper, Michael Gabriel, committee member
Logan, Timothy M., 1961-, committee member
Florida State University, degree granting institution
College of Arts and Sciences, degree granting college
Department of Chemistry and Biochemistry, degree granting department
Type of Resource: text
Genre: Text
Issuance: monographic
Date Issued: 2016
Publisher: Florida State University
Florida State University
Place of Publication: Tallahassee, Florida
Physical Form: computer
online resource
Extent: 1 online resource (111 pages)
Language(s): English
Abstract/Description: Histone variants and post-translational modifications (PTMs) are known to play central roles in genome regulation and maintenance. Quantitavely characterization of the variants and the associated PTMs is the first step to understand their biological functions. However, many variants and the PTM combinations are inaccessible by antibody-based methods or bottom-up tandem mass spectrometry. For many, the only tractable approach is with intact protein top-down tandem mass spectrometry. In this dissertation, a method of identification of histone H4 proteoforms is developed, revealing the challenge of top-down proteomics. Then a method of proteoform identification and relative quantitation of histones H2A and H2B by FT-ICR MS and MS/MS is developed, yielding quantitative identification of all detected H2A and H2B isobaric and isomeric proteoforms with a label-free approach in HeLa. The method is further extended to 1) normal and HIV-infected U937 cells; 2) the Fluorescence Ubiquitination Cell Cycle Indicator (FUCCI) stem cells sorted into early G1, late G1, S, and G2/M phases; 3) MDA-MB-231 breast cancer cells synchronized to S and M phases. The top-down MS/MS approach provides a path forward for more extensive elucidation of the biological roles of many previously unstudied histone variants and PTMs.
Identifier: FSU_2016SU_Dang_fsu_0071E_13350 (IID)
Submitted Note: A Dissertation submitted to the Department of Chemistry and Biochemistry in partial fulfillment of the requirements for the degree of Doctor of Philosophy.
Degree Awarded: Summer Semester 2016.
Date of Defense: June 27, 2016.
Bibliography Note: Includes bibliographical references.
Advisory Committee: Alan G. Marshall, Professor Directing Dissertation; David M. Gilbert, University Representative; Michael G. Roper, Committee Member; Timothy M. Logan, Committee Member.
Subject(s): Chemistry
Chemistry, Analytic
Persistent Link to This Record: http://purl.flvc.org/fsu/fd/FSU_2016SU_Dang_fsu_0071E_13350
Use and Reproduction: This Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). The copyright in theses and dissertations completed at Florida State University is held by the students who author them.
Host Institution: FSU

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Dang, X. (2016). Characterization of Protein Sequence Variants and Posttranlational Modifications by Top-down Fourier Transform Ion Cyclotron Resonance Mass Spectrometry. Retrieved from http://purl.flvc.org/fsu/fd/FSU_2016SU_Dang_fsu_0071E_13350