{"id":4226,"date":"2018-09-18T11:57:57","date_gmt":"2018-09-18T16:57:57","guid":{"rendered":"https:\/\/uwm.edu\/physics\/?post_type=tribe_events&#038;eventDate=2018-11-02#038;p=4219"},"modified":"2019-01-16T08:47:18","modified_gmt":"2019-01-16T14:47:18","slug":"colloquium-thomas-perkins","status":"publish","type":"tribe_events","link":"https:\/\/uwm.edu\/physics\/event\/colloquium-thomas-perkins\/","title":{"rendered":"Physics Colloquium &#8211; Thomas T. Perkins"},"content":{"rendered":"<p><strong>Thomas T. Perkins<\/strong>, JILA<\/p>\n<p><strong>Watching Individual Proteins Unfold and Refold Using 1-\u00b5s Resolution Force Spectroscopy<\/strong><\/p>\n<p>Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. To achieve state-of-the-art performance, we integrated several recent technical advances that improve the precision, stability, and accuracy of AFM-based single molecule force spectroscopy. Using modified cantilevers optimized for 1-\u00b5s resolution, we reexamined the unfolding of individual bacteriorhodopsin (bR) molecules in native lipid bilayers.  The experimental data revealed the unfolding pathway in unprecedented detail.  Numerous newly detected intermediates\u2014many separated by as few as 2\u20133 amino acids\u2014exhibited complex dynamics, including frequent refolding and state occupancies of &lt;10 \u00b5s. Equilibrium measurements between such states enabled the folding free-energy landscape to be deduced.  These results sharpen the picture of the mechanical unfolding of bR.  Finally, recent efforts to improve the quantity and quality of AFM studies of diverse biomolecules, including nucleic-acid structures and globular proteins, will be discussed.<\/p>\n<p>Event posting flyer <a href=\"https:\/\/uwm.edu\/physics\/wp-content\/uploads\/sites\/63\/2018\/10\/Thomas-Perkins-11-02-2018-Posting-Flyer.pdf\">here<\/a><\/p>\n","protected":false},"excerpt":{"rendered":"<p><strong>Thomas T. Perkins<\/strong>, JILA<\/p>\n<p><strong>Watching Individual Proteins Unfold and Refold Using 1-\u00b5s Resolution Force Spectroscopy<\/strong><\/p>\n<p>Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. To achieve state-of-the-art performance, we integrated several recent technical advances that improve the precision, stability, and accuracy of AFM-based single molecule force spectroscopy.<\/p>\n","protected":false},"author":9647,"featured_media":0,"template":"","meta":{"_acf_changed":false,"_tribe_events_status":"","_tribe_events_status_reason":"","_tribe_events_is_hybrid":"","_tribe_events_is_virtual":"","_tribe_events_virtual_video_source":"","_tribe_events_virtual_embed_video":"","_tribe_events_virtual_linked_button_text":"","_tribe_events_virtual_linked_button":"","_tribe_events_virtual_show_embed_at":"","_tribe_events_virtual_show_embed_to":[],"_tribe_events_virtual_show_on_event":"","_tribe_events_virtual_show_on_views":"","_tribe_events_virtual_url":"","footnotes":"","uwm_wg_additional_authors":[]},"tags":[],"tribe_events_cat":[58],"class_list":["post-4226","tribe_events","type-tribe_events","status-publish","hentry","tribe_events_cat-physics-colloquia","cat_physics-colloquia"],"yoast_head":"<!-- This site is optimized with the Yoast SEO Premium plugin v27.5 (Yoast SEO v27.5) - https:\/\/yoast.com\/product\/yoast-seo-premium-wordpress\/ -->\n<title>Physics &amp; Astronomy<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/uwm.edu\/physics\/event\/colloquium-thomas-perkins\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Physics Colloquium - Thomas T. Perkins\" \/>\n<meta property=\"og:description\" content=\"Thomas T. Perkins, JILA  Watching Individual Proteins Unfold and Refold Using 1-\u00b5s Resolution Force Spectroscopy  Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. To achieve state-of-the-art performance, we integrated several recent technical advances that improve the precision, stability, and accuracy of AFM-based single molecule force spectroscopy.\" \/>\n<meta property=\"og:url\" content=\"https:\/\/uwm.edu\/physics\/event\/colloquium-thomas-perkins\/\" \/>\n<meta property=\"og:site_name\" content=\"Physics &amp; Astronomy\" \/>\n<meta property=\"article:modified_time\" content=\"2019-01-16T14:47:18+00:00\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:label1\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data1\" content=\"1 minute\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\\\/\\\/schema.org\",\"@graph\":[{\"@type\":\"WebPage\",\"@id\":\"https:\\\/\\\/uwm.edu\\\/physics\\\/event\\\/colloquium-thomas-perkins\\\/\",\"url\":\"https:\\\/\\\/uwm.edu\\\/physics\\\/event\\\/colloquium-thomas-perkins\\\/\",\"name\":\"Physics Colloquium - Thomas T. 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Perkins, JILA  Watching Individual Proteins Unfold and Refold Using 1-\u00b5s Resolution Force Spectroscopy  Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. 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