{"id":1098,"date":"2017-12-03T17:55:15","date_gmt":"2017-12-04T01:55:15","guid":{"rendered":"http:\/\/blogs.oregonstate.edu\/inspiration\/?p=1098"},"modified":"2018-02-11T20:59:49","modified_gmt":"2018-02-12T04:59:49","slug":"exploring-proteins-turf-tirf","status":"publish","type":"post","link":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/2017\/12\/03\/exploring-proteins-turf-tirf\/","title":{"rendered":"Exploring a protein’s turf with TIRF"},"content":{"rendered":"

Investigating Otoferlin
\n<\/strong><\/p>\n

Otoferlin is a protein required for hearing. Mutations in its gene sequence have been linked to hereditary deafness, affecting 360 million people globally, including 32 million children. Recently graduated PhD candidate Nicole Hams has spent the last few years working to characterize the activity of Otoferlin using TIRF microscopy. There are approximately 20,000 protein-coding genes in humans, and many of these proteins are integral to processes occurring in cells at all times. Proteins are encoded by genes, which are comprised of DNA; when mutations in the gene sequence occur, diseases can arise. Mutations in DNA that give rise to disease are the focus of critical biomedical research. \u201cIf DNA is the frame of the car, proteins are the engine,\u201d explains Nicole. Studying proteins can provide insight into how diseases begin and progress, with the strategic design of therapies to treat disease founded on our understanding of protein structure and function.<\/p>\n

Studying proteins<\/strong><\/p>\n

Proteins are difficult to study because they\u2019re so small: at an average size of ~2 nanometers (0.000000002 meters!), specific tools are required for visualization. Enter TIRF. Total Internal Reflection Fluorescence is a form of microscopy enabling scientists like Nicole to observe proteins tagged with a fluorescent marker. One reason TIRF is so useful is that it permits visualization of samples at the single molecule level. Fluorescently-tagged proteins light up as bright dots against a dark background, indicating that you have your protein.<\/p>\n

Another reason why proteins are hard to study is that in many cases, parts of the protein are not soluble in water (especially if part of the protein is embedded in the fatty cell membrane). Trying to purify protein out of a membrane is extremely challenging. Often, it\u2019s more feasible for scientists to study smaller, soluble fragments of the larger protein. Targeted studies using truncated, soluble portions of protein offer valuable information about protein function, but they don\u2019t tell the whole story. \u201cWorking with a portion of the protein gives great insight into binding or interaction partners, but some information about the function of the whole protein is lost when you study fragments.\u201d By studying the whole protein, Nicole explains, \u201cwe can offer insight into mechanisms that lead to deafness as a result of mutations.\u201d<\/p>\n

Challenges and rewards of research<\/strong><\/p>\n

Nicole cites being the first person in her lab to pursue single molecule studies as a meaningful achievement in her graduate career. She became immersed in tinkering with the new TIRF instrument, learning from the ground up how to develop new experiments. Working with cells containing Otoferlin, in a process known as tissue culture, required Nicole to be in lab at unusual hours, often for long periods of time, to make sure that the cells wouldn\u2019t die. \u201cThe cells do not wait on you,\u201d she explains, adding, \u201ceven if they\u2019re ready at 3am.\u201d Sometimes Nicole worked nights in order to get time on the TIRF. \u201cIf you love it, it\u2019s not a sacrifice.\u201d<\/p>\n

Why grad school?<\/strong><\/p>\n

As an undergraduate student studying Agricultural Biochemistry at the University of Missouri, Nicole worked in a soybean lab investigating nitrogen fixation, and knew she wanted to pursue research further. She had worked in a lab work since high school, but didn\u2019t realize it was a path she could pursue, instead convinced that she wanted to go to medical school. Nicole\u2019s mom encouraged her to pursue research, because she knew that it was something she enjoyed, and her undergraduate advisor (who completed his post-doc at OSU) suggested that she apply to OSU. She feels lucky to have found an advisor like Colin Johnson, and stresses the importance of finding a mentor who is personally vested in their graduate student\u2019s success.<\/p>\n

Besides lab work…<\/strong><\/p>\n

In addition to research, Nicole has been actively involved in outreach to the community, serving as Educational Chair of the local NAACP Chapter. Following completion of her PhD, Nicole intends to continue giving back to the community, by establishing a scholarship program for underrepresented students. Nicole remembers a time when she was told and believed that she wasn\u2019t good enough, and while she was able to overcome this discouraging dialogue, she has observed that many students do not find the necessary support to pursue higher education. Her goal is to reach students who don\u2019t realize they have potential, and provide them with resources for success.<\/p>\n

Tune in on December 3rd\u00a0 at 7pm to 88.7 KBVR Corvallis<\/strong> or stream the show live right here<\/a>\u00a0to hear more about Nicole\u2019s journey through graduate school!<\/p>\n

Thanks for reading!<\/p>\n

You can download Nicole’s iTunes Podcast Episode!<\/a><\/p>\n

Earlier in the show we discussed current events, specifically how the tax bill moving through the House and Senate impact students. Please see our references and sources<\/a> for more information.<\/p>\n","protected":false},"excerpt":{"rendered":"

Investigating Otoferlin Otoferlin is a protein required for hearing. Mutations in its gene sequence have been linked to hereditary deafness, affecting 360 million people globally, including 32 million children. Recently graduated PhD candidate Nicole Hams has spent the last few years working to characterize the activity of Otoferlin using TIRF microscopy. There are approximately 20,000 […]<\/p>\n","protected":false},"author":8081,"featured_media":0,"comment_status":"open","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"footnotes":""},"categories":[644798,1375,17224,742798,1305525,745514],"tags":[],"class_list":["post-1098","post","type-post","status-publish","format-standard","hentry","category-biochemistry-and-biophysics","category-college-of-science","category-linus-pauling-institute","category-molecular-and-cell-biology","category-science-communication","category-stem-outreach"],"_links":{"self":[{"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/posts\/1098","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/users\/8081"}],"replies":[{"embeddable":true,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/comments?post=1098"}],"version-history":[{"count":6,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/posts\/1098\/revisions"}],"predecessor-version":[{"id":1186,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/posts\/1098\/revisions\/1186"}],"wp:attachment":[{"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/media?parent=1098"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/categories?post=1098"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/dev.blogs.oregonstate.edu\/inspiration\/wp-json\/wp\/v2\/tags?post=1098"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}