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<title>PHYSorg.com: PHYSorg news tagged with: protein structure</title>
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     <title>Scientists reveal key structure from ebola virus</title>
   	 <description>Scientists at The Scripps Research Institute have determined the structure of a critical protein from the Ebola virus, which, though rare, is one of the deadliest viruses on the planet killing between 50 and 90 percent of those infected. Described in the advance, online Early Edition of the journal Proceedings of the National Academy of Sciences (PNAS), the research reveals how a key component of the Ebola virus, called VP35, blocks the human immune system, allowing the virus uncontrolled replication. The structure represents a major step forward in understanding how the deadly virus works, and may be useful in the development of potential treatments for those infected.</description>
     <link>http://www.physorg.com/news179514235.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Tue, 08 Dec 2009 17:14:32 EST</pubDate>
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     <title>Green tea chemical combined with another may hold promise for treatment of brain disorders</title>
   	 <description>Scientists at Boston Biomedical Research Institute (BBRI) and the University of Pennsylvania have found that combining two chemicals, one of which is the  green tea component EGCG, can prevent and destroy a variety of protein structures known as amyloids. Amyloids are the primary culprits in fatal brain disorders such as Alzheimer's, Huntington's, and Parkinson's diseases.  Their study, published in the current issue of Nature Chemical Biology (December 2009), may ultimately contribute to future therapies for these diseases.</description>
     <link>http://www.physorg.com/news179060136.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 03 Dec 2009 10:57:46 EST</pubDate>
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     <title>The hidden lives of proteins</title>
   	 <description>An important Brandeis study appearing in the December 3 issue of Nature raises the curtain on the hidden lives of proteins at the atomic level. The study reports that for the first time, researchers used x-ray crystallography and nuclear magnetic resonance (NMR) techniques to directly visualize protein structures essential for catalysis at the rare high-energy state. The study also showed how the motions of these rare, or hidden, structures collectively, directly contribute to enzyme catalysis.</description>
     <link>http://www.physorg.com/news178987418.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 02 Dec 2009 15:30:01 EST</pubDate>
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     <title>Designer molecule detects tiny amounts of cyanide, then glows</title>
   	 <description>(PhysOrg.com) -- A small molecule designed to detect cyanide in water samples works quickly, is easy to use, and glows under ultraviolet or "black" light. Although the fluorescent molecule is not yet ready for market, its Indiana University Bloomington creators report in the Journal of the American Chemical Society that the tool is already able to sense cyanide below the toxicity threshold established by the World Health Organization.</description>
     <link>http://www.physorg.com/news175359189.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 21 Oct 2009 15:54:34 EST</pubDate>
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     <title>Dysfunctional protein dynamics behind neurological disease?</title>
   	 <description>Researchers at Lund University, Sweden, have taken a snapshot of proteins changing shape, sticking together and creating structures that are believed to trigger deadly processes in the nervous system. The discovery opens the possibility of designing drugs for a devastating neurological disease, ALS.</description>
     <link>http://www.physorg.com/news174649594.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Tue, 13 Oct 2009 11:03:56 EST</pubDate>
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     <title>How the 100th protein structure solved at Diamond impacts our understanding of how insects smell</title>
   	 <description>New research announced today, Wednesday 30th September, by a team of leading scientists working with the UK's national Synchrotron, Diamond Light Source, could have a significant impact on the development and refinement of new eco-friendly pest control methods for worldwide agriculture.</description>
     <link>http://www.physorg.com/news173452384.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 29 Sep 2009 14:40:01 EST</pubDate>
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     <title>Building a complete metabolic model</title>
   	 <description>Investigators at Burnham Institute for Medical Research, University of California, San Diego, The Scripps Research Institute, Genomics Institute of the Novartis Research Foundation and other institutions have constructed a complete model, including three dimensional protein structures, of the central metabolic network of the bacterium Thermotoga maritima (T. maritima). </description>
     <link>http://www.physorg.com/news172419921.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 17 Sep 2009 15:28:15 EST</pubDate>
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     <title>Landmark study sheds new light on human chromosomal birth defects</title>
   	 <description>Using yeast genetics and a novel scheme to selectively remove a single protein from the cell division process called meiosis, a cell biologist at The Florida State University found that when a key molecular player known as Pds5 goes missing, chromosomes fail to segregate and pair up properly, and birth defects such as Down syndrome can result.</description>
     <link>http://www.physorg.com/news172334309.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 16 Sep 2009 16:30:01 EST</pubDate>
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     <title>Disordered proteins sensitive to environment, sequence changes</title>
   	 <description>(PhysOrg.com) -- Research published by a team of Indiana University bioinformaticists has shown quantitatively the influence of small sequence changes and environmental conditions on the disordered regions of a protein. </description>
     <link>http://www.physorg.com/news172153088.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 14 Sep 2009 13:19:44 EST</pubDate>
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     <title>Chemists create protein structure database</title>
   	 <description>(PhysOrg.com) -- Any chemist with access to the Internet can now use a powerful tool to help them accurately identify the structure of a protein, thanks to recently published work led by Harold A. Scheraga, Cornell's Todd Professor of Chemistry Emeritus.</description>
     <link>http://www.physorg.com/news171738311.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 09 Sep 2009 18:30:02 EST</pubDate>
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     <title>A Cell's Private Life: Researchers Peer Inside a Hidden Protein</title>
   	 <description>(PhysOrg.com) -- To understand the molecular machinery of the human body, scientists have to be able to observe the structure of cellular proteins. This has been particularly challenging for those proteins embedded in cellular membranes. Now researchers from the Yale School of Medicine have established a novel way to peer inside this hidden universe, obtaining the first close-up look at a membrane-embedded potassium ion channel that, when defective, can cause high blood pressure or epilepsy. The research appears August 30 in Nature's Advance Online Publication.</description>
     <link>http://www.physorg.com/news170609059.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Sun, 30 Aug 2009 13:00:01 EST</pubDate>
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     <title>Research reveals how cells tell time</title>
   	 <description>The fuzzy pale mold that lines the glass tubes in Dr. Yi Liu's lab doesn't look much like a clock. But this fungus has an internal, cell-based timekeeper nearly as sophisticated as a human's, allowing UT Southwestern Medical Center physiologists to study easily the biochemistry and genetics of body clocks, or circadian rhythms. </description>
     <link>http://www.physorg.com/news163700594.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Mon, 08 Jun 2009 17:24:15 EST</pubDate>
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     <title>Determining success or failure in cholesterol-controlling drugs</title>
   	 <description>Researchers at the University of California, San Diego have discovered that a complex network of interactions between drugs and the proteins with which they bind can explain adverse drug effects. Their findings suggest that adverse drug effects might be minimized by using single or multiple drug therapies in order to fine-tune multiple off-target interactions.</description>
     <link>http://www.physorg.com/news161609790.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 15 May 2009 12:37:16 EST</pubDate>
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     <title>Chameleon-like camouflage: 'Nano-camo' for fashionistas and environmentalists</title>
   	 <description>(PhysOrg.com) --  Certain fish species blend with their environment by changing color. Sandia National Laboratories researchers have demonstrated that, in theory, they could cause synthetic materials to change color like fish do.</description>
     <link>http://www.physorg.com/news159198454.html</link>
	 <category>Nanotechnology</category>
	 <pubDate>Fri, 17 Apr 2009 14:47:58 EST</pubDate>
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     <title>Unfolding 'nature's origami'</title>
   	 <description>Sometimes known as "nature's origami", the way that proteins fold is vital to ensuring they function correctly. But researchers at the University of Leeds have discovered this is a 'hit and miss' process, with proteins potentially folding wrongly many times before they form the correct structure for their intended purpose.</description>
     <link>http://www.physorg.com/news155233369.html</link>
	 <category>Biology</category>
	 <pubDate>Mon, 02 Mar 2009 16:23:17 EST</pubDate>
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     <title>In race to predict protein structure, computers take lead</title>
   	 <description>A flood of data is emerging from genome research, including sequence data on proteins. To help science keep pace with this flow of knowledge, computer scientists, biophysicists and biochemists across the world have been developing advanced technologies to help derive accurately and quickly the three-dimensional structure of proteins from this data. </description>
     <link>http://www.physorg.com/news151252682.html</link>
	 <category>Technology</category>
	 <pubDate>Thu, 15 Jan 2009 14:38:02 EST</pubDate>
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     <title>Protein 'tubules' free avian flu virus from immune recognition</title>
   	 <description>A protein found in the virulent avian influenza virus strain called H5N1 forms tiny tubules in which it "hides" the pieces of double-stranded RNA formed during viral infection, which otherwise would prompt an antiviral immune response from infected cells, said Baylor College of Medicine researchers in an online report in the journal Nature.</description>
     <link>http://www.physorg.com/news145110178.html</link>
	 <category>Biology</category>
	 <pubDate>Wed, 05 Nov 2008 12:22:58 EST</pubDate>
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     <title>Improved technique determines structure in membrane proteins</title>
   	 <description>Understanding the form and function of certain proteins in the human body is becoming faster and easier, thanks to the work of researchers at the University of Illinois. </description>
     <link>http://www.physorg.com/news138179978.html</link>
	 <category>Chemistry</category>
	 <pubDate>Sun, 17 Aug 2008 08:19:38 EST</pubDate>
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