{"id":30631,"date":"2016-04-20T08:00:03","date_gmt":"2016-04-20T13:00:03","guid":{"rendered":"https:\/\/uwm.edu\/news\/?p=30631"},"modified":"2017-02-27T12:20:00","modified_gmt":"2017-02-27T18:20:00","slug":"uncloaking-the-chemistry-of-life","status":"publish","type":"post","link":"https:\/\/uwm.edu\/news\/uncloaking-the-chemistry-of-life\/","title":{"rendered":"Uncloaking the chemistry of life"},"content":{"rendered":"<p>Living organisms operate like factories, producing continuous chemical reactions, with proteins serving as the laborers. Every process that sustains life depends on these complex molecules.<\/p>\n<p>Discovering how proteins do their jobs holds incredible potential for improving lives. But unraveling their functions depends on seeing how the atoms are arranged and how they change during reactions. Until recently, only a fraction of the world\u2019s proteins could be observed with current technology.<\/p>\n<p>Now, two UW-Milwaukee scientists have helped usher in a new age of unmasking proteins, using a tool that images extremely small objects with unprecedented speed and clarity. In a groundbreaking experiment, UW-Milwaukee physicist Marius Schmidt and his doctoral student, Jason Tenboer, became the first to witness a protein changing in real time with the X-Ray Free Electron Laser, or XFEL. The feat has opened the door to resolving what Schmidt calls \u201csome of the grand challenges of biology \u2013 understanding the molecular basis of life.\u201d<\/p>\n<h3>The nano-moment of truth<\/h3>\n<p>A protein is far smaller than a single cell. About 3,000 different proteins operate in the common bacterium E. coli, for example.<\/p>\n<p>For the past 60 years, the only way to examine proteins in 3-D was with X-ray crystallography. The process shoots X-rays at crystallized proteins, which diffract light and create patterns of dots the way shaking a paintbrush sprays drops on a wall.<\/p>\n<p>The pattern provides a fingerprint for that protein. The millions of data points can be mathematically reconstructed to form a 3-D image of the protein\u2019s molecular structure at a single point in time \u2013 a still snapshot.<\/p>\n<p>But this method works with less\u00a0than 20 percent of proteins \u2013 only those that crystallize in a small enough size \u2013 and it can\u2019t capture them in action. For that, scientists need a laser with split-second X-ray pulses.<\/p>\n<p>They found the tool they needed at the Stanford Linear Accelerator Center in Menlo Park, California.<\/p>\n<p>With a light source that\u2019s a billion times brighter than any other equipment, the XFEL transforms X-ray crystallography into a kind of high-definition video, providing ultraslow-motion of extremely rapid events.<\/p>\n<figure id=\"attachment_30633\" aria-describedby=\"caption-attachment-30633\" style=\"width: 300px\" class=\"wp-caption alignleft\"><img loading=\"lazy\" decoding=\"async\" class=\"wp-image-30633 size-medium\" src=\"https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins-300x200.jpg\" alt=\"proteins\" width=\"300\" height=\"200\" srcset=\"https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins-300x200.jpg 300w, https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins-768x512.jpg 768w, https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins-1024x683.jpg 1024w, https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins-750x500.jpg 750w, https:\/\/uwm.edu\/news\/wp-content\/uploads\/sites\/41\/2016\/03\/proteins.jpg 1440w\" sizes=\"auto, (max-width: 300px) 100vw, 300px\" \/><figcaption id=\"caption-attachment-30633\" class=\"wp-caption-text\">Professor Marius Schmidt (left) and doctoral student Jason Tenboer. (51ÁÔÆæ Photo\/Troye Fox)<\/figcaption><\/figure>\n<p>Schmidt and Tenboer spent about six months growing protein crystals at UW-Milwaukee before heading west. Deciding it was too risky to fly the delicate cargo, they carefully packed the specimens into a climate-controlled van for the long drive to California.<\/p>\n<h3>In a quadrillionth of a second<\/h3>\n<p>Once there, they worked with a team of 34 other scientists from nine institutions to put the XFEL to the test. The group included four additional UW-Milwaukee researchers: Abbas Ourmazd, Peter Schwander, Chris Kupitz and Jennifer Scales.<\/p>\n<p>The team induced a chemical reaction in a protein crystal the size of a bacterium and then bombarded it with X-rays. With data generated by the signature \u201csprays\u201d of photons, they created high-resolution \u201cmaps\u201d documenting electrons in the protein molecules shifting during the reaction.<\/p>\n<p>\u201cBiology happens at inconceivably short time spans,\u201d Tenboer said. \u201cSo the XFEL allows us to do time-resolved studies of proteins in action down to the femtosecond time scale \u2013 that\u2019s 10<sup>-15<\/sup>\u00a0of a second.\u201d<\/p>\n<p>Since their first experiment, Schmidt and Tenboer have conducted a second experiment, making them the first to observe a chemical reaction unfold among multiple proteins working together.<\/p>\n<p>\u201cThis study shows that the molecular details of life\u2019s chemistry can be followed using X-ray laser nano-crystallography,\u201d Schmidt said, \u201cwhich puts some of biology\u2019s most sought-after goals within reach.\u201d<\/p>\n<p>Schmidt and Tenboer\u2019s paper was published last year in the journal Science. The UW-Milwaukee physicists named here are members of a prestigious $25 million BioXFEL Science and Technology Center funded by the National Science Foundation.<\/p>\n<p>Researchers from UW-Milwaukee and SLAC were joined by researchers from Arizona State University; Lawrence Livermore National Laboratory; University of Hamburg and DESY in Hamburg, Germany; State University of New York, Buffalo; University of Chicago; and Imperial College in London. The work was supported by the National Science Foundation, National Institutes of Health and Lawrence Livermore National Laboratory.<\/p>\n<p>___<\/p>\n<p>Read the full 2016 UW-Milwaukee\u00a0<em><a href=\"https:\/\/uwm.edu\/researchreport\/\">Research Report<\/a>.<\/em><\/p>\n","protected":false},"excerpt":{"rendered":"<p>51ÁÔÆæ researchers Marius Schmidt and Jason Tenboer harnessed X-Ray Free Electron Laser technology and became the first people to witness proteins changing in real time. <\/p>\n","protected":false},"author":836,"featured_media":30632,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"page-templates\/flexible-layout-posts.php","format":"standard","meta":{"_acf_changed":false,"footnotes":"","uwm_wg_additional_authors":[]},"categories":[174,175],"tags":[],"section":[140,139],"display_categories":[116],"related-coverage":[],"uwmnews-feed":[158,161],"class_list":["post-30631","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news","category-research","section-science","section-science-technology","display_categories-top-story-section","uwmnews-feed-letters-science","uwmnews-feed-hard-science"],"yoast_head":"<!-- This site is optimized with the Yoast SEO Premium plugin v27.3 (Yoast SEO v27.3) - https:\/\/yoast.com\/product\/yoast-seo-premium-wordpress\/ -->\n<title>Uncloaking the chemistry of life<\/title>\n<meta name=\"description\" content=\"51ÁÔÆæ researchers Marius Schmidt and Jason 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