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	<title>Los Alamos National Laboratory News</title>
	<description>Los Alamos National Laboratory News for </description>
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	<language>en-us</language>
	<copyright>Copyright 2008 (C) University of California</copyright>
	<lastbuilddate>Wed,  9 Jul 2008 00:57:56 -0600</lastbuilddate>
	<webmaster>www-core@lanl.gov</webmaster>
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	<title>Los Alamos National Laboratory: The World's Greatest Science Protecting America</title>
	<url>http://www.lanl.gov/images/lalogo.gif</url>
	<link>http://www.lanl.gov</link>
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<title>Reagentless Optical Biosensor</title>
<description>A reagentless optical biosensor comprises a cartridge with a pathogen recognition membrane, including a planar optical waveguide and grating. A binding event triggers an optical signal. An aperture permits introduction of a sample. The cartridge is inserted into a handheld reader comprising a power source, a laser for illuminating the waveguide, a means for detecting the optical signal, and electronics for processing said signal and giving an output reading.</description>
<link>http://www.lanl.gov/orgs/tt/license/technologies/index.php?fuseaction=home.viewTechnology&amp;id=491</link>
<pubdate>Fri, 27 Jun 2008 00:00:00 -0600</pubdate>
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<title>Superfolder Green Fluorescent Protein (Gfp)  Mutations that Improve the Folding of GFP Fused to Poorly Folded Polypeptides</title>
<description>A form of &quot;superfolding&quot; green fluorescent protein (GFP), designated GFPSF, has been produced and has been associated with mutations identified as S30R, Y39N, N105T, Y145F, I171V, and A206V. A library of mutants of a poorly folding protein, bullfrog H-subunit ferritin, was ligated in-frame with GFP in a linearized plasmid vector, and the GFP fusion libary was expressed by induction with IPTG.  Each resulting cell colony expressed a slightly different version of ferrritin as a GFP fusion, and colonies expressing better-folded versions of ferritin contained more copies of correctly folded, higher fluorescence GFP.  Starting with a known variation, GFP3, directed evolution involving successive in vitro recombination and mutation was employed in this manner, keeping the sequence of the poorly folded ferritin domain constant while varying the sequence of the GFP domain, until no further brightness was detected in resulting cell colonies of E. coli.  Clones of the resulting colonies were then sequenced to identify the concensus mutations.  The resulting superfolder GFPSF is many times brighter as a fusion with ferritin than the starting GFP3.  Applications include the use of GFPSF as a direct reporter of expression level, unaffected by folding.</description>
<link>http://www.lanl.gov/orgs/tt/license/technologies/index.php?fuseaction=home.viewTechnology&amp;id=494</link>
<pubdate>Fri, 27 Jun 2008 00:00:00 -0600</pubdate>
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<title>Reversible Modification of Carbon Nanotube Electronic Properties for Sensors and Electronics Applications</title>
<description>The invention describes a novel method for a reversible biosensor with carbon nanotubes serving as a novel platform for sensitive detection.&amp;nbsp; Sensor applications may use either an electronic or optical signal for transduction.&amp;nbsp; The invention functions through reversible modification of nanotube electronic properties and behavior and, in addition to applications in biosensors, may also be used for tunable nanotube electronics.</description>
<link>http://www.lanl.gov/orgs/tt/license/technologies/index.php?fuseaction=home.viewTechnology&amp;id=591</link>
<pubdate>Fri, 27 Jun 2008 00:00:00 -0600</pubdate>
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<title>Protein Folding Reporter System Using Insertion Vectors</title>
<description>Obtaining soluble, well-folded recombinant proteins for downstream applications requires screening large numbers of protein variants and testing many expression or refolding conditions.&amp;nbsp; Recombinant proteins are attached to reporter proteins, which give a functional 'signal' when the recombinant protein is correctly folded.&amp;nbsp; Existing folding reporters fuse the N-terminus of the&amp;nbsp;reporter to the C-terminus of the test protein.&amp;nbsp; This approach generates significant false-positives due to test protein truncations.&amp;nbsp; This invention&amp;nbsp;gets around this problem by sandwiching test proteins between two domains of a reporter protein with an easily selected function.&amp;nbsp; Correct folding and full-length expression&amp;nbsp;of&amp;nbsp;test proteins allows functional activity of the reporter.&amp;nbsp; This strategy has been successfully used with two&amp;nbsp;different reporter systems,&amp;nbsp;green fluorescent protein (GFP) and dihydrofolate reductase (DHFR), at LANL.&amp;nbsp;Additional robustness is added to this new system by coupling it with the improved folding of the&amp;nbsp;LANL GFP Superfolder.&amp;nbsp;&amp;nbsp;&amp;nbsp;Several Superfolder mutants can be employed to allow for variable folding stringencies, giving users of this technology the opportunity to adjust how well the test protein must be folded in order to generate a positive signal.</description>
<link>http://www.lanl.gov/orgs/tt/license/technologies/index.php?fuseaction=home.viewTechnology&amp;id=592</link>
<pubdate>Fri, 27 Jun 2008 00:00:00 -0600</pubdate>
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<title>Chemical Synthesis of Water-Soluble, Chiral Conducting Polymer Complexes</title>
<description>This invention describes novel water-soluble, chiral conducting polymer complex and method for their chemical synthesis. The complexes consist of a conducting polymer in combination with a water-soluble polymer. Chirality is achieved using a proprietary process. These water-soluble complexes have advantages over organic soluble because of their ease of synthesis and processing and they are environmentally friendly. Using chemical synthesis over electrochemical synthesis methods has the advantages of being able to scale up and its simplicity and cost savings.</description>
<link>http://www.lanl.gov/orgs/tt/license/technologies/index.php?fuseaction=home.viewTechnology&amp;id=158</link>
<pubdate>Wed, 25 Jun 2008 00:00:00 -0600</pubdate>
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