{"id":355,"date":"2014-07-07T14:07:24","date_gmt":"2014-07-07T18:07:24","guid":{"rendered":"http:\/\/research.chemistry.ohio-state.edu\/foster\/?page_id=355"},"modified":"2018-07-13T08:35:35","modified_gmt":"2018-07-13T12:35:35","slug":"dissertations","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/foster.281\/dissertations\/","title":{"rendered":"Dissertations"},"content":{"rendered":"<h2>PhD Dissertations<\/h2>\n<ul>\n<li><a hreaf=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu15005487808765&#038;disposition=attachment\">Eric Danhart (2017)<\/a> Protein and RNA structure and function by NMR spectroscopy<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1471621708\">Brandon Crowe (2016)<\/a> <span id=\"P10_TITLE\" class=\"display_only\">Structural Features of Proteins Involved in Pfu RNase P or Recruitment of Viral Genomes to Human Chromatin<\/span><\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1429547886\">Elihu Ihms (2015)<\/a> <span id=\"P10_TITLE\" class=\"display_only\">Integrative Investigation and Modeling of Macromolecular Complexes<\/span><\/li>\n<li><a title=\"Ian Kleckner (2011)\" href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1313460041\">Ian Kleckner (2011)<\/a> Thermodynamic, Kinetic, and Dynamics Studies of the Allosteric Ligand-Responsive Regulatory Protein TRAP<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view.cgi?acc%5Fnum=osu1267762846\">Yiren (Joy) Xu (2010<\/a><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1267762846\">)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1267762846&amp;disposition=attachment\">PDF<\/a>) Structure and interactions of archaeal RNase P proteins : RPP29 and RPP21<\/li>\n<li><a title=\"Ross Wilson (2009)\" href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1260765086\">Ross Wilson (2009)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1260765086&amp;disposition=attachment\">PDF<\/a>) Structure and function in archaeal RNase P and the SMK box riboswitch<\/li>\n<li><a href=\"https:\/\/etd.ohiolink.edu\/ap\/10?0::NO:10:P10_ACCESSION_NUM:osu1205431343\">Carlos Amero (2008)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1205431343&amp;disposition=attachment\">PDF<\/a>) Protein function study by NMR spectroscopy<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc%5Fnum=osu1172778957\">Hari Kamadurai (2007)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1172778957&amp;disposition=attachment\">PDF<\/a>) Mechanistic insights into catalysis and allosteric enzyme activation in bacteriophage lambda integrase<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc%5Fnum=osu1111429539\">Craig McElroy (2005)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1111429539&amp;disposition=attachment\">PDF<\/a>) Dynamics and function : mechanistic studies of the gene regulatory proteins TRAP and anti-TRAP<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc%5Fnum=osu1117552357\">Will Boomershire (2005)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1117552357&amp;disposition=attachment\">PDF<\/a>) Structure and interactions of archaeal RNase P proteins Mth Rpp29 and Pfu Rpp21<\/li>\n<li><a href=\"http:\/\/rave.ohiolink.edu\/etdc\/view?acc_num=osu1111655332\">Srisunder Subramaniam (2005)<\/a> (<a href=\"https:\/\/etd.ohiolink.edu\/!etd.send_file?accession=osu1111655332&amp;disposition=attachment\">PDF<\/a>) Studies of conformational changes and dynamics accompanying substrate recognition, allostery and catalysis in bacteriophage lambda integrase<\/li>\n<li><a href=\"http:\/\/osu.worldcat.org\/oclc\/56748961\">Douglas Byerly (2002)<\/a> Structure and dynamics of ligand binding to E. coli peptide deformylase<\/li>\n<li><a href=\"http:\/\/osu.worldcat.org\/oclc\/47108412\">Hee-Jung Kim (2000)<\/a> I. studies of AD5 E3-14.7K, an Adenoviral Inhibitor of TNF receptor- and FAS-mediated Apoptosis : II. investigation of interactions between Cyclin-dependent Kinase 4 and tumor suppressor p16(INK4A)<\/li>\n<\/ul>\n<h2>BS Theses<\/h2>\n<ul>\n<li><a href=\"https:\/\/chemistry.osu.edu\/~foster.281\/Dissertations\/ISmith_Honors%20Thesis.doc\">Ian Smith (BS, 2011)<\/a> Application of Site-directed Metal Chelation Techniques to Structure Determination of Pyrococcus furiosus RNase P<\/li>\n<li><a href=\"http:\/\/hdl.handle.net\/1811\/46676\">David Smith (BS, 2010) <\/a>Purification and biophysical study of RNase P proteins 21 and 29 from Methanocaldococcus jannaschii<\/li>\n<li><a href=\"http:\/\/hdl.handle.net\/1811\/24608\">Amber Simmons (BS, 2007)<\/a> Inhibition and thermodynamics of Escherichia coli peptide<\/li>\n<li><a href=\"http:\/\/hdl.handle.net\/1811\/6585\">Christopher Bohlen (BS, 2006) <\/a>NMR study of Rpp30, an archaeal RNase P protein<\/li>\n<\/ul>\n","protected":false},"excerpt":{"rendered":"<p>PhD Dissertations Eric Danhart (2017) Protein and RNA structure and function by NMR spectroscopy Brandon Crowe (2016) Structural Features of Proteins Involved in Pfu RNase P or Recruitment of Viral Genomes to Human Chromatin Elihu Ihms (2015) Integrative Investigation and<\/p>\n","protected":false},"author":3,"featured_media":0,"parent":0,"menu_order":4,"comment_status":"closed","ping_status":"closed","template":"","meta":{"jetpack_post_was_ever_published":false,"footnotes":""},"class_list":["post-355","page","type-page","status-publish","hentry"],"jetpack_sharing_enabled":true,"jetpack_shortlink":"https:\/\/wp.me\/P7sxod-5J","jetpack-related-posts":[{"id":829,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/fosterlab-resources\/","url_meta":{"origin":355,"position":0},"title":"FosterLab Resources","author":"Mark Foster","date":"March 2, 2016","format":false,"excerpt":"Dissertations Lab Calendar Software SLAM Instrumentation Funding Opportunities (http:\/\/go.osu.edu\/funding ) \u00a0","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]},{"id":632,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/research-areas\/protein-nucleic-acid-interactions\/","url_meta":{"origin":355,"position":1},"title":"Protein-Nucleic Acid Interactions","author":"Mark Foster","date":"January 17, 2016","format":false,"excerpt":"Protein-Nucleic Acid Interactions TRAP\u00a0 \u2666 \u00a0RNase P \u00a0\u2666\u00a0 Loz1 \u2666 \u00a0tRNA Editing\u00a0 \u2666\u00a0 Tyrosine Recombinases TRAP The ring-forming oligomeric Bacillus trp RNA binding attenuation protein (TRAP), defines a paradigm for gene regulation by ligand-mediated alteration of the structure of non-coding RNA, and for mechanisms of both homotropic and heterotropic allostery.\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2016\/01\/pxpa-shifting-194x300.png?resize=350%2C200&ssl=1","width":350,"height":200},"classes":[]},{"id":16,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/publications\/","url_meta":{"origin":355,"position":2},"title":"Publications","author":"Eric Danhart","date":"August 8, 2013","format":false,"excerpt":"Selected Publications Ma X, Baktina M, Shulgina I, Cantara WA, Nagy ABK, Goto Y, Suga H, Foster MP, Musier-Forsyth K. Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain. Nucleic Acids Res. 2023 May 8; 51(8):3988-3999. doi: 10.1093\/nar\/gkad192. Li W, Norris AS, Lichtenthal K, Kelly S, Ihms\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"rid_logo","src":"https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2013\/08\/rid_logo.gif?ssl=1&resize=350%2C200","width":350,"height":200},"classes":[]},{"id":628,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/research-areas\/allosteric-gene-regulation\/","url_meta":{"origin":355,"position":3},"title":"Allosteric Gene Regulation","author":"Mark Foster","date":"January 17, 2016","format":false,"excerpt":"Mechanisms of Allosteric Gene Regulation TRAP \u00a0\u2666\u00a0 Anti-TRAP \u2666\u00a0 SMK Riboswitch TRAP The ring-forming oligomeric Bacillus trp RNA binding attenuation protein (TRAP), defines a paradigm for gene regulation by ligand-mediated alteration of the structure of non-coding RNA, and for mechanisms of both homotropic and heterotropic allostery. Undecameric (11-mer) TRAP serves\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2013\/08\/ATdodecamer-150x150.png?resize=350%2C200&ssl=1","width":350,"height":200},"classes":[]},{"id":8,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/members-2023\/","url_meta":{"origin":355,"position":4},"title":"Foster Lab Members","author":"Mark Foster","date":"August 8, 2013","format":false,"excerpt":"\u00a0 Mark P. Foster, PhD ProfessorDepartment of Chemistry and BiochemistryThe Ohio State University484 West 12th Ave, Columbus OH 43210EmailB.S.\u00a0University of Illinois, 1987Ph.D University of Utah, 1993Postdoctoral Fellow, The Scripps Research Institute, 1993-1997 \u00a0 \u00a0 Antonia Duran Ohio State Biochemistry Program, Email Describing the structural basis of protein-protein interactions provides valuable\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2023\/08\/image-20230727-193300-178586a0-1024x769.jpeg?resize=350%2C200&ssl=1","width":350,"height":200,"srcset":"https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2023\/08\/image-20230727-193300-178586a0-1024x769.jpeg?resize=350%2C200&ssl=1 1x, https:\/\/i0.wp.com\/research.cbc.osu.edu\/foster.281\/wp-content\/uploads\/2023\/08\/image-20230727-193300-178586a0-1024x769.jpeg?resize=525%2C300&ssl=1 1.5x"},"classes":[]},{"id":1846,"url":"https:\/\/research.cbc.osu.edu\/foster.281\/great-resources-for-learning-nmr-nuclear-magnetic-resonance\/","url_meta":{"origin":355,"position":5},"title":"Great resources for learning NMR (Nuclear Magnetic Resonance)","author":"Mark Foster","date":"February 5, 2023","format":false,"excerpt":"John Keeler's great book Understanding NMR Spectroscopy (2010)(Amazon), which he amazingly makes mostly available on line as PDFs: http:\/\/www-keeler.ch.cam.ac.uk. That\u2019s a really good place to start. For a more in-depth treatment, Spin Dynamics (2008) by Levitt (Amazon) More tailored to application of NMR to proteins, in solution:Protein NMR Spectroscopy. Principles\u2026","rel":"","context":"Similar post","block_context":{"text":"Similar post","link":""},"img":{"alt_text":"","src":"","width":0,"height":0},"classes":[]}],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/355","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/comments?post=355"}],"version-history":[{"count":8,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/355\/revisions"}],"predecessor-version":[{"id":1435,"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/pages\/355\/revisions\/1435"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/foster.281\/wp-json\/wp\/v2\/media?parent=355"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}