{"id":9483,"date":"2017-03-24T11:49:28","date_gmt":"2017-03-24T10:49:28","guid":{"rendered":"https:\/\/news.embl.de\/?p=9483"},"modified":"2024-03-22T13:39:38","modified_gmt":"2024-03-22T12:39:38","slug":"futures-dark-proteome","status":"publish","type":"post","link":"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/","title":{"rendered":"Futures: The dark proteome"},"content":{"rendered":"\n<div class=\"wp-block-image wp-image-9484 size-full vf-u-width__30\"><figure class=\"vf-figure  | vf-figure--align vf-figure--align-inline-start  \"><a href=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2017\/03\/lemke_edward.jpg\"><img loading=\"lazy\" decoding=\"async\" width=\"150\" height=\"150\" class=\"vf-figure__image\" src=\"https:\/\/news.embl.de\/wp-content\/uploads\/2017\/03\/lemke_edward.jpg\" alt=\"\" class=\"wp-image-9484\"\/><\/a><figcaption class=\"vf-figure__caption\">EMBL group leader <a href=\"http:\/\/www.embl.de\/research\/units\/scb\/lemke\/index.html\">Edward Lemke<\/a>. PHOTO: EMBL<\/figcaption><\/figure><\/div>\n\n\n\n<p>The conventional view of proteins is that they have a well-defined three-dimensional structure, which makes them like perfectly optimised engines for carrying out a particular task. Determining a protein\u2019s structure can help us understand more about its function and makes it easier to identify compounds that might modify its activity, which can be important in developing new drugs. However, about a third of proteins in the human body are part of what we call the dark proteome \u2013 a group of proteins whose structures cannot easily be determined, because they\u2019re intrinsically disordered proteins (IDPs). IDPs don\u2019t have a well-defined structure at all \u2013 they\u2019re more like flexible strings. For a long time they couldn\u2019t be studied because they don\u2019t form crystals \u2013 as required for X-ray crystallography \u2013 and other techniques like electron microscopy don\u2019t work well on flexible molecules.<\/p>\n\n\n\n<p>More recently, it\u2019s been discovered that IDPs are involved in the formation of membraneless organelles \u2013 regions of a cell that perform certain functions and contain different chemicals to their surroundings, but without any membrane physically separating them from the rest of the cell. The way these organelles work is still mysterious, but they\u2019re thought to play an important role in processes like cell division. Recent developments \u2013 including advanced fluorescence microscopy techniques \u2013 are making it possible to figure this out.<\/p>\n\n\n\n<blockquote class=\"vf-blockquote\"><p>About a third of proteins in the human body are part of the dark proteome<\/p><\/blockquote>\n\n\n\n<p>One way IDPs can be studied is by modifying the DNA of a cell so that an IDP is expressed with a molecule of green fluorescent protein (GFP) attached to it. This molecule fluoresces when exposed to certain wavelengths of light, revealing the position of the IDP in the cell. Unfortunately GFP itself is quite large, so it prevents us from studying IDPs at the high resolution we would like to. We\u2019re currently experimenting with alternative labelling strategies involving smaller semi-synthetic fluorescent molecules. In ten years I\u2019d love to have a situation where no one would think of using GFP any more.<\/p>\n\n\n\n<p>To truly understand the way IDPs function and how they interact with other molecules, we need to visualise them at a near atomistic level. We don\u2019t have that kind of resolution yet \u2013 being able to do that is a ten-year vision or maybe even longer.<\/p>\n\n\n<div class=\"vf-box vf-box--normal vf-box-theme--primary\">\n<p class=\"vf-box__text\" style=\"float: left; margin: 5px 16px 0 0;\"><img decoding=\"async\" src=\"https:\/\/news.embl.de\/wp-content\/uploads\/2017\/03\/erc-logo150x150.jpg\"\/><\/p>\n<p class=\"vf-box__text\" style=\"margin-top: 0;\">The European Research Council (ERC) is a European funding body that offers substantial five-year grants to support researchers at all stages of their careers. Inspired by&nbsp;the ERC\u2019s tenth anniversary in 2017, we asked some of EMBL\u2019s ERC grantees to look ahead another ten years and share their vision for their field of research.<\/p>\n<p class=\"vf-box__text\" style=\"margin-top: 40px;\"><a href=\"http:\/\/www.embl.de\/research\/faculty\/erc-investigators\/\">Find out more about EMBL&#8217;s ERC grantees<\/a>.<\/p>\n<p class=\"vf-box__text\"><a href=\"https:\/\/news.embl.de\/tag\/futures\/?_ga=1.233145306.592483598.1486366032\">More&nbsp;articles in EMBL&#8217;s Futures series<\/a>.<\/p>\n<p class=\"vf-box__text\"><\/p><\/div>\n","protected":false},"excerpt":{"rendered":"<p>ERC grantee Edward Lemke shares his vision for the next ten years<\/p>\n","protected":false},"author":45,"featured_media":9487,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[2,17591],"tags":[495,43,358,79,45,35],"embl_taxonomy":[],"class_list":["post-9483","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-science","category-science-technology","tag-future","tag-heidelberg","tag-lemke","tag-microscopy","tag-proteomics","tag-structural-biology"],"acf":{"article_intro":"<p>As part of a series marking the tenth anniversary of the European Research Council, ERC grantee Edward Lemke\u00a0shares his\u00a0vision for the next ten years<\/p>\n","related_links":[{"link_description":"Lemke Group","link_url":"http:\/\/www.embl.de\/research\/units\/scb\/lemke\/index.html"},{"link_description":"ERC","link_url":"http:\/\/erc.europa.eu"}],"article_sources":[{"source_description":"","source_link_url":"http:\/\/"}],"vf_locked":false,"featured":false,"color":"#007B53","show_featured_image":false,"source_article":false,"in_this_article":false,"press_contact":"None"},"embl_taxonomy_terms":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.2 - https:\/\/yoast.com\/wordpress\/plugins\/seo\/ -->\n<title>Futures: The dark proteome | EMBL<\/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:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Futures: The dark proteome | EMBL\" \/>\n<meta property=\"og:description\" content=\"ERC grantee Edward Lemke shares his vision for the next ten years\" \/>\n<meta property=\"og:url\" content=\"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/\" \/>\n<meta property=\"og:site_name\" content=\"EMBL\" \/>\n<meta property=\"article:publisher\" content=\"https:\/\/www.facebook.com\/embl.org\/\" \/>\n<meta property=\"article:published_time\" content=\"2017-03-24T10:49:28+00:00\" \/>\n<meta property=\"article:modified_time\" content=\"2024-03-22T12:39:38+00:00\" \/>\n<meta property=\"og:image\" content=\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2017\/03\/Lemke.jpg\" \/>\n\t<meta property=\"og:image:width\" content=\"620\" \/>\n\t<meta property=\"og:image:height\" content=\"426\" \/>\n\t<meta property=\"og:image:type\" content=\"image\/jpeg\" \/>\n<meta name=\"author\" content=\"Edward Dadswell\" \/>\n<meta name=\"twitter:card\" content=\"summary_large_image\" \/>\n<meta name=\"twitter:creator\" content=\"@embl\" \/>\n<meta name=\"twitter:site\" content=\"@embl\" \/>\n<meta name=\"twitter:label1\" content=\"Written by\" \/>\n\t<meta name=\"twitter:data1\" content=\"Edward Dadswell\" \/>\n\t<meta name=\"twitter:label2\" content=\"Est. reading time\" \/>\n\t<meta name=\"twitter:data2\" content=\"2 minutes\" \/>\n<script type=\"application\/ld+json\" class=\"yoast-schema-graph\">{\"@context\":\"https:\/\/schema.org\",\"@graph\":[{\"@type\":\"NewsArticle\",\"@id\":\"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/#article\",\"isPartOf\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/\"},\"author\":{\"name\":\"Edward Dadswell\",\"@id\":\"https:\/\/www.embl.org\/news\/#\/schema\/person\/d09d98139462e79513cfc92f6bcfaba7\"},\"headline\":\"Futures: The dark proteome\",\"datePublished\":\"2017-03-24T10:49:28+00:00\",\"dateModified\":\"2024-03-22T12:39:38+00:00\",\"mainEntityOfPage\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/\"},\"wordCount\":474,\"publisher\":{\"@id\":\"https:\/\/www.embl.org\/news\/#organization\"},\"image\":{\"@id\":\"https:\/\/www.embl.org\/news\/science\/futures-dark-proteome\/#primaryimage\"},\"thumbnailUrl\":\"https:\/\/www.embl.org\/news\/wp-content\/uploads\/2017\/03\/Lemke.jpg\",\"keywords\":[\"future\",\"heidelberg\",\"lemke\",\"microscopy\",\"proteomics\",\"structural biology\"],\"articleSection\":[\"Science\",\"Science &amp; 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