{"id":81,"date":"2016-11-15T01:23:52","date_gmt":"2016-11-15T01:23:52","guid":{"rendered":"https:\/\/sites.bioe.uw.edu\/dratner\/?page_id=81"},"modified":"2023-07-13T08:42:08","modified_gmt":"2023-07-13T15:42:08","slug":"test","status":"publish","type":"page","link":"https:\/\/sites.bioe.uw.edu\/daggett\/","title":{"rendered":"Home"},"content":{"rendered":"<div id=\"carousel-81-1\" class=\"carousel slide captions-simple\" data-ride=\"carousel\" data-interval=\"false\" role=\"region\" aria-label=\"manual image\" aria-roledescription=\"carousel\" aria-live=\"polite\">\n<div class=\"carousel-inner\">\n<figure class=\"carousel-item active\" aria-roledescription=\"slide\" aria-label=\"Side A flips from B Strand\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/07\/1cd0_neu_2_sideA_flips_from_Bstrand.gif\" class=\"d-block w-100\" alt=\"Side A flips from B Strand\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Characterizing the \u03b1-sheet Structure<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/Biofilm-e1687795645563.png\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Bacterial Amyloid in Biofilms<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/Amyloidogenic-Protein-Examples-e1687795691962.png\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>\u03b1-sheet in Amyloid Diseases<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/Paranjapye-TEM-biofilms-e1687796499648.jpg\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Amyloid Inhibitor Design<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/SOD1-Thermal-Unfolding-Pathways-e1687795824925.jpeg\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Protein Folding-Unfolding Pathways<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/comp_no_border-e1687795791233.jpg\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Conformational Changes in Amyloidogenesis<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/peptide-and-protein-design-e1687795856200.png\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Peptide and Protein Design<\/p>\n<\/figcaption><\/figure>\n<figure class=\"carousel-item\" aria-roledescription=\"slide\" aria-label=\"\"><img decoding=\"async\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/06\/DIVE_usage-e1687795890437.png\" class=\"d-block w-100\" alt=\"\"><figcaption class=\"carousel-caption d-none d-sm-block w-40\">\n<p>Bioinformatics &amp; Software Development<\/p>\n<\/figcaption><\/figure>\n<\/div>\n<p><button class=\"carousel-control-prev\" href=\"#carousel-81-1\" type=\"button\" data-slide=\"prev\"><span class=\"carousel-control-prev-icon\" aria-hidden=\"true\"><\/span><span class=\"sr-only\">Previous image<\/span><\/button><button class=\"carousel-control-next\" href=\"#carousel-81-1\" type=\"button\" data-slide=\"next\"><span class=\"carousel-control-next-icon\" aria-hidden=\"true\"><\/span><span class=\"sr-only\">Next image<\/span><\/button><\/div>\n<h4>Welcome to the Daggett Research Group.<\/h4>\n<figure id=\"attachment_1631\" aria-describedby=\"caption-attachment-1631\" style=\"width: 300px\" class=\"figure figure-caption wp-caption alignright\"><img loading=\"lazy\" decoding=\"async\" class=\"wp-image-1631 size-medium\" src=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/07\/valerie_daggett_candid-300x200.jpg\" alt=\"Valerie Daggett\" width=\"300\" height=\"200\" srcset=\"https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/07\/valerie_daggett_candid-300x200.jpg 300w, https:\/\/sites.bioe.uw.edu\/daggett\/wp-content\/uploads\/sites\/47\/2023\/07\/valerie_daggett_candid.jpg 337w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><figcaption id=\"caption-attachment-1631\" class=\"wp-caption-text\"><strong>Valerie Daggett Ph.d.<\/strong> <br \/><em>Principle Investigator<\/em> <br \/>Professor, UW Bioengineering<br \/>Founder and CEO, AltPep Corp. <\/figcaption><\/figure>\n<p>Our group is currently focused on protein unfolding and disease where we combine both computational and experimental approaches. We have developed a database to simulate representatives of all known protein folds, an effort we call <a href=\"http:\/\/www.dynameomics.org\/\">Dynameomics<\/a>, which has led to the largest collection of simulations and protein structures in the world.<\/p>\n<p>We also pursue simulations of protein unfolding related to amyloidogenesis. We found that amyloidogenic peptides and proteins under amyloidogenic conditions changed structure and formed a novel, nonstandard secondary structure, which we dubbed <a href=\"https:\/\/sites.uw.edu\/daggett-lab\/research\/experimental\/%ce%b1-sheet-in-amyloid-diseases\/\">\u03b1-sheet<\/a>. We proposed that <strong>\u03b1-sheet structure is linked to toxicity during amyloidogenesis<\/strong>, and have developed an \u03b1-sheet library to test our peptide inhibitor designs in 1) mammalian amyloid disease systems, and 2) bacteria that use amyloid fibrils for biofilm stability to evade the host immune response and antibiotics. Our compounds inhibit aggregation and toxicity by binding the toxic oligomers that form en route to mature amyloid.<\/p>\n","protected":false},"excerpt":{"rendered":"<p>Welcome!<\/p>\n","protected":false},"author":1,"featured_media":0,"parent":0,"menu_order":2,"comment_status":"closed","ping_status":"closed","template":"","meta":{"footnotes":""},"class_list":["post-81","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/pages\/81","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/users\/1"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/comments?post=81"}],"version-history":[{"count":20,"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/pages\/81\/revisions"}],"predecessor-version":[{"id":1989,"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/pages\/81\/revisions\/1989"}],"wp:attachment":[{"href":"https:\/\/sites.bioe.uw.edu\/daggett\/wp-json\/wp\/v2\/media?parent=81"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}