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Structural and Dynamic Studies of Supramolecular Assemblies by Solid State NMR Spectroscopy

Gao, Min
http://rave.ohiolink.edu/etdc/view?acc_num=osu1385135235

Abstract Details

, Doctor of Philosophy, Ohio State University, Chemistry.
Solid-state nuclear magnetic resonance (SSNMR) is one of the most widely used spectroscopic techniques to probe high resolution atomic level details for macromolecules, membrane proteins, and insoluble, non-crystalline proteins like amyloid fibrils. In this thesis, the application of SSNMR runs from self-assembled nanotubes to DNA-protein complex-chromatin. In collaboration with Dr. Parquette from department of Chemistry at OSU, we synthesized a series of isotope labeled small organic molecules able to form homogeneous nanostructures by dissolving in water. Applying two dimensional 13C-13C and 13C-15N correlations experiments on uniformly, diluted and mixed isotope labeled samples, intermolecular and intramolecular distances were extracted. In combination with EM, XRD, and MD simulation data, the energy stable nanotube structure was proposed at atomic resolution. The application of SSNMR was extended to study cellular polymer-chromatin, which was in collaboration with Dr. Poirier from department of Physics at OSU. Chromatin is a highly conserved DNA-protein complex that plays a vital role in the processes of DNA transcription, translation and replication. The basic building block of chromatin is the nucleosome core particle, which consists of ~147 bp of DNA wrapping around the histone protein octamer containing two copies each of histones H2A, H2B, H3 and H4. The histone proteins contain well-structured helical segments as well as flexible tails that account for nearly 30% of the sequences in total. These histone tails have been linked to the assembly of nucleosomes into chromatin fibers. Due to the complexity of large nucleosome arrays, very few atomic-level studies which have been carried out to understand the role of histone tails in facilitating DNA compaction have relied on indirect approaches such as hydrogen/deuterium exchange solution NMR or computational methods. Here we present the results of initial MAS NMR studies designed to provide high-resolution insights into the flexible tail domains of histones H3 and H4 within 17-mer nucleosome arrays under experimental conditions designed to mimic different degrees of DNA compaction in chromatin by using different concentrations of Mg2+. Our main findings to date are that the same set of residues exhibiting dynamic disorder for single nucleosomes remain flexible in the context of large arrays, and that the residues comprising the flexible H3 and H4 tails in the open state of chromatin also remain largely flexible in the compacted state.
Christopher Jaroniec (Advisor)
Chemistry
Solid state NMR, Chromatin, Self-assembly, Structure, Dynamic

Recommended Citations

Citations

  • Gao, M. (n.d.). Structural and Dynamic Studies of Supramolecular Assemblies by Solid State NMR Spectroscopy [Doctoral dissertation, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1385135235

    APA Style (7th edition)

  • Gao, Min. Structural and Dynamic Studies of Supramolecular Assemblies by Solid State NMR Spectroscopy . Ohio State University, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1385135235.

    MLA Style (8th edition)

  • Gao, Min. "Structural and Dynamic Studies of Supramolecular Assemblies by Solid State NMR Spectroscopy ." Doctoral dissertation, Ohio State University. Accessed MAY 08, 2024. http://rave.ohiolink.edu/etdc/view?acc_num=osu1385135235

    Chicago Manual of Style (17th edition)

osu1385135235
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