{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/80497"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/80497","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Lighting Up Life: Fluorescence Studies of the Shaker Potassium Ion Channel and Myosin v in Action","abstract":"\"The other protein I studied is myosin V which walks bipedally along actin filaments taking steps which displace the center of mass 37 nm per step. A controversy over the nature of this movement was settled earlier this year by other members of our laboratory when they showed that myosin V processes in a hand-over-hand manner, with each of the heads alternating in the leading and trailing positions. To do this, they developed a new technique which they called FIONA for Fluorescence Imaging with One Nanometer Accuracy which allowed them to localize individual molecules of myosin V to within 1.5 nut on the surface of a microscope cover slip. I have extended and applied FIONA to a mutant of myosin V with a molecule of the enhanced Green Fluorescent Protein (eGFP) fused to one head of the dieter. I demonstrated that eGFP is suitable to use with FIONA, confirm the hand-over-hand model of myosin procession, and argue that in aggregate, the data on myosin's steps from our lab implies that myosin V adopts an asymmetric, \"\"telemark skier,\"\" configuration between steps. (Abstract shortened by UMI.).\"","abstract_html":""The other protein I studied is myosin V which walks bipedally along actin filaments taking steps which displace the center of mass 37 nm per step. A controversy over the nature of this movement was settled earlier this year by other members of our laboratory when they showed that myosin V processes in a hand-over-hand manner, with each of the heads alternating in the leading and trailing positions. To do this, they developed a new technique which they called FIONA for Fluorescence Imaging with One Nanometer Accuracy which allowed them to localize individual molecules of myosin V to within 1.5 nut on the surface of a microscope cover slip. I have extended and applied FIONA to a mutant of myosin V with a molecule of the enhanced Green Fluorescent Protein (eGFP) fused to one head of the dieter. I demonstrated that eGFP is suitable to use with FIONA, confirm the hand-over-hand model of myosin procession, and argue that in aggregate, the data on myosin's steps from our lab implies that myosin V adopts an asymmetric, ""telemark skier,"" configuration between steps. (Abstract shortened by UMI.)."","abstract_has_math":false,"creators":["Snyder, Gregory E."],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Physics","degree_department":null,"school":null,"contributors":["Selvin, Paul R."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2015,"date_issued":"2015-09-25T20:02:46Z","date_published":"2015-09-25T20:02:46Z","updated_at":"2026-07-22T22:26:14Z","subjects":["Biophysics, General"],"languages":["eng"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["(MiAaPQ)AAI3101972"],"render_values":[{"text":"(MiAaPQ)AAI3101972","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/80497","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Selvin, Paul R."]},{"key":"dc:creator","label":"Author","values":["Snyder, Gregory E."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2015-09-25T20:02:46Z","10000-01-01","2003"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Physics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biophysics, General"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["http://hdl.handle.net/2142/80497","(MiAaPQ)AAI3101972"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["\"The other protein I studied is myosin V which walks bipedally along actin filaments taking steps which displace the center of mass 37 nm per step. A controversy over the nature of this movement was settled earlier this year by other members of our laboratory when they showed that myosin V processes in a hand-over-hand manner, with each of the heads alternating in the leading and trailing positions. To do this, they developed a new technique which they called FIONA for Fluorescence Imaging with One Nanometer Accuracy which allowed them to localize individual molecules of myosin V to within 1.5 nut on the surface of a microscope cover slip. I have extended and applied FIONA to a mutant of myosin V with a molecule of the enhanced Green Fluorescent Protein (eGFP) fused to one head of the dieter. I demonstrated that eGFP is suitable to use with FIONA, confirm the hand-over-hand model of myosin procession, and argue that in aggregate, the data on myosin's steps from our lab implies that myosin V adopts an asymmetric, \"\"telemark skier,\"\" configuration between steps. (Abstract shortened by UMI.).\"","Made available in DSpace on 2015-09-25T20:02:46Z (GMT). No. of bitstreams: 2 license.txt: 4848 bytes, checksum: 96035ab3f5e1c23cc7138a224ce498bd (MD5) 3101972.pdf: 4402337 bytes, checksum: 65ff7bc7588f5430d12855e5fa82cf3c (MD5) Previous issue date: 2003","Embargo set by: Seth Robbins for item 81779 Lift date: Forever Reason: Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","Restricted to the U of I community idenfinitely during batch ingest of legacy ETDs","U of I Only","91 p.","Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2003."]},{"key":"dc:title","label":"Title","values":["Lighting Up Life: Fluorescence Studies of the Shaker Potassium Ion Channel and Myosin v in Action"]}]}],"canonical_facts":{"dc:contributor":["Selvin, Paul R."],"dc:creator":["Snyder, Gregory E."],"dc:date":["2015-09-25T20:02:46Z","10000-01-01","2003"],"dc:description":["\"The other protein I studied is myosin V which walks bipedally along actin filaments taking steps which displace the center of mass 37 nm per step. A controversy over the nature of this movement was settled earlier this year by other members of our laboratory when they showed that myosin V processes in a hand-over-hand manner, with each of the heads alternating in the leading and trailing positions. To do this, they developed a new technique which they called FIONA for Fluorescence Imaging with One Nanometer Accuracy which allowed them to localize individual molecules of myosin V to within 1.5 nut on the surface of a microscope cover slip. I have extended and applied FIONA to a mutant of myosin V with a molecule of the enhanced Green Fluorescent Protein (eGFP) fused to one head of the dieter. I demonstrated that eGFP is suitable to use with FIONA, confirm the hand-over-hand model of myosin procession, and argue that in aggregate, the data on myosin's steps from our lab implies that myosin V adopts an asymmetric, \"\"telemark skier,\"\" configuration between steps. (Abstract shortened by UMI.).\"","Made available in DSpace on 2015-09-25T20:02:46Z (GMT). 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