{"id":41,"date":"2011-07-26T15:37:49","date_gmt":"2011-07-26T15:37:49","guid":{"rendered":"http:\/\/research.chemistry.ohio-state.edu\/ottesen\/?page_id=41"},"modified":"2015-11-03T15:24:29","modified_gmt":"2015-11-03T20:24:29","slug":"research","status":"publish","type":"page","link":"https:\/\/research.cbc.osu.edu\/ottesen.1\/research\/","title":{"rendered":"Ottesen Lab Research"},"content":{"rendered":"

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\"Artistic<\/a>

Artistic rendering by Ruixuan (Ryan) Yu<\/figcaption><\/figure>\n

Background<\/h4>\n

The Ottesen Laboratory is\u00a0interested in protein engineering as applied to solving biological problems and constructing new functional materials. Our projects are in three main areas: 1) Using the tools of chemical biology to understand\u00a0histone modifications as the foundation of biological function; 2) Bridging the gap between synthetic proteins and biology; developing methods to introduce synthetic proteins into eukaryotic cells to study them in the cellular context, 3) Building new functional nanomaterials using the tools of biomolecular chemistry.<\/p>\n

Chemical Tools for Histone Synthesis<\/h4>\n

In a eukaryotic organism, DNA is organized into nucleosomes by wrapping around cores of histone proteins like thread around a spool. \u00a0These “spools” are then put away and organized into higher order structures. \u00a0Small physical changes to these spools can set them apart, to identify them as the targets for biological activity such as activating a gene, or as a site of DNA repair. These changes are chemical modifications to histone proteins.<\/p>\n

Our laboratory uses several different approaches to build histone proteins with distinct modification sets, then build\u00a0them back into nucleosomes in order to understand how their functions have changed. \u00a0More information about\u00a0our synthetic toolkit\u00a0can be found here: Chemical Tools for Histone Synthesis<\/a><\/p>\n

We are particularly interested in understanding how chemical changes in the folded core of the nucleosome affects the inherent structure and dynamics of the nucleosome, and have a long-standing collaboration with the Poirier Laboratory in the Department of Physics. \u00a0Please see our publication list for recent work in this area.<\/p>\n

Crossing the Biological Barrier: Protein Chemistry in the Cell<\/h4>\n

With modern techniques in protein chemistry, we can treat proteins as large organic molecules with control down to the individual atom. \u00a0However, we are typically limited to studying these elegant constructions in isolation in \u00a0in vitro<\/em> settings. \u00a0The ultimate goal of a biomolecular chemist has to be bridging the gap between\u00a0protein chemistry and\u00a0the cellular environment. The Ottesen Laboratory has two ongoing projects in this area.<\/p>\n

Engineered Hybrid Nanomaterials<\/h4>\n

Proteins are amazing materials with the ability to carry out very specific chemical reactions in a complex environment in response to cues from their surroundings. While protein engineers have long sought to capture this activity into human-designed systems, we have fallen short. \u00a0Nucleic acids are simple materials and can be designed into dynamic programmable nanodevices, but they have minimal function. \u00a0In collaboration with the Castro Laboratory in Mechanical and Aerospace Engineering, we are working to bridge this gap by designing\u00a0protein-DNA hybrid nanomaterials with environmentally-sensitive function.<\/p>\n

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Collaborations<\/a><\/h4>\n

Information for Undergraduate Researchers<\/a><\/h4>\n

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Background The Ottesen Laboratory is\u00a0interested in protein engineering as applied to solving biological problems and constructing new functional materials. Our projects are in three main areas: 1) Using the tools of chemical biology to understand\u00a0histone modifications as the foundation of biological function; 2) Bridging the gap between synthetic proteins and biology; developing methods to introduce … Continue reading Ottesen Lab Research<\/span> →<\/span><\/a><\/p>\n","protected":false},"author":6,"featured_media":0,"parent":0,"menu_order":0,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-41","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/41","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/users\/6"}],"replies":[{"embeddable":true,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/comments?post=41"}],"version-history":[{"count":3,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/41\/revisions"}],"predecessor-version":[{"id":243,"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/pages\/41\/revisions\/243"}],"wp:attachment":[{"href":"https:\/\/research.cbc.osu.edu\/ottesen.1\/wp-json\/wp\/v2\/media?parent=41"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}