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	<title><![CDATA[BOL: Related items]]></title>
	<link>https://bioinformaticsonline.com/related/4943?offset=370</link>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/news/view/11144/scientists-map-17294-proteins-produced-in-human-body</guid>
	<pubDate>Thu, 29 May 2014 01:57:55 -0500</pubDate>
	<link>https://bioinformaticsonline.com/news/view/11144/scientists-map-17294-proteins-produced-in-human-body</link>
	<title><![CDATA[Scientists map 17,294 proteins produced in human body]]></title>
	<description><![CDATA[<p>Indian scientists missed the genomic profiling bus, but they've more than made up for it by creating the first human proteome map which is an extension of the genomic study. Till now, here is no direct equivalent for the human proteome. But recently two groups present mass spectrometry-based analysis of human tissues, body fluids and cells mapping the large majority of the human proteome.</p><p>The Indian scientists working in Bangalore, along with their American counterparts, have mapped more than 17,000 proteins in 30 organs of the human body. Just like the human genome was sequenced around the turn of the millennium, this is an equivalent mapping of the human proteome.<br /><br />The researcher estimated there are around 20,500 proteins in the human body. These scientists have profiled around 17,294, which account for around 84% of the total proteins. Apart from this, the team also traced around 2,500 of 3,000 proteins that had been categorised as "missing proteins".</p><p>The work, done by group of Indian scientists, and Johns Hopkins University, published in the renowned journal Nature ( http://www.nature.com/nature/journal/v509/n7502/full/nature13302.html ). Of the 72 people who worked on the project, 46 are Indians.</p><p>Reference:</p><p>http://www.nature.com/nature/journal/v509/n7502/full/nature13302.html</p><p>http://www.proteinatlas.org/ -The antibody-based Human Protein Atlas programme</p><p>http://www.humanproteomemap.org/ -Proteogenomic analysis by identifying translated proteins from annotated pseudogenes, non-coding RNAs and untranslated regions.</p><p>https://www.proteomicsdb.org/ -Assembled protein evidence for 18,097 genes in ProteomicsDB</p><p>&nbsp;</p>]]></description>
	<dc:creator>Jit</dc:creator>
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<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/file/view/13911/amino-acid-flash-tutorial</guid>
	<pubDate>Mon, 11 Aug 2014 08:58:17 -0500</pubDate>
	<link>https://bioinformaticsonline.com/file/view/13911/amino-acid-flash-tutorial</link>
	<title><![CDATA[Amino Acid Flash Tutorial]]></title>
	<description><![CDATA[<p>Protein is a part of every cell in your body, and no other nutrient plays as many different roles in keeping you alive and healthy. Protein is the building block of our body, and amino acids are the main areas of interest. We have emphasized on all 20 amino acids in this documentary movie. This documentary has been developed that emphasize on chemical structure, chemical formula, IUPAC name and other detail information of all 20 amino acids with the voice, picture with interactive button. This will be helpful for the entire biology and bioinformatics student.</p><p>How to run?</p><p>You need to install flash player or open it with web browser ( I guess you have installed flash plugin) to play.</p><p>Comment below if you like it. Thanks</p>]]></description>
	<dc:creator>Jit</dc:creator>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/31278/metapred2cs</guid>
	<pubDate>Fri, 03 Mar 2017 05:15:07 -0600</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/31278/metapred2cs</link>
	<title><![CDATA[MetaPred2CS]]></title>
	<description><![CDATA[<p style="text-align: justify;"><strong>MetaPred2CS Web server&nbsp;</strong>is a meta-predictor based on&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/17160063">Support Vector Machine (SVM)</a>&nbsp;that combines 6 individual sequence based protein-protein interaction prediction methods to predict&nbsp;<strong>prokaryotic two-component system&nbsp;</strong>protein-protein interactions (PPIs). The methods implemented in MetaPred2CS are 2 co-evolutionary methods:&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/11933068">in-silico two hybrid (i2h)</a>&nbsp;and&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/11707606">mirror tree (MT)</a>&nbsp;methods and 4 genomics context based methods:&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/15947018">phylogenetic profiling (PP)</a>,&nbsp;<a href="http://www.ncbi.nlm.nih.gov/pubmed/10573422">gene fusion (GF)</a>,&nbsp;<a href="http://www.ploscompbiol.org/article/info%3Adoi%2F10.1371%2Fjournal.pcbi.0030043">gene neighbourhood (GN)</a>&nbsp;and and&nbsp;<a href="http://www.ploscompbiol.org/article/info%3Adoi%2F10.1371%2Fjournal.pcbi.0030043">gene operon methods (GO)</a>.</p>
<p>&nbsp;http://metapred2cs.ibers.aber.ac.uk/</p><p>Address of the bookmark: <a href="https://github.com/martinjvickers/MetaPred2CS" rel="nofollow">https://github.com/martinjvickers/MetaPred2CS</a></p>]]></description>
	<dc:creator>Manisha Mishra</dc:creator>
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	<guid isPermaLink="true">https://bioinformaticsonline.com/bookmarks/view/35787/protein-subcellular-localization-prediction</guid>
	<pubDate>Thu, 01 Mar 2018 06:20:47 -0600</pubDate>
	<link>https://bioinformaticsonline.com/bookmarks/view/35787/protein-subcellular-localization-prediction</link>
	<title><![CDATA[Protein Subcellular Localization Prediction]]></title>
	<description><![CDATA[<p>Assigning subcellular localization to a protein is an important step towards elucidating its interaction partners, function, and potential role(s) in the cellular machinery. Computational tools offer an attractive complement to time-consuming and laborious experimental methods.</p>
<p>http://abi.inf.uni-tuebingen.de/Services/YLoc/webloc.cgi</p><p>Address of the bookmark: <a href="https://abi.inf.uni-tuebingen.de/Research/Systems%20Biology/protein-subcellular-localization" rel="nofollow">https://abi.inf.uni-tuebingen.de/Research/Systems%20Biology/protein-subcellular-localization</a></p>]]></description>
	<dc:creator>Poonam Mahapatra</dc:creator>
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<item>
	<guid isPermaLink="true">https://bioinformaticsonline.com/pages/view/36398/tools-for-protein-protein-docking</guid>
	<pubDate>Wed, 25 Apr 2018 05:15:53 -0500</pubDate>
	<link>https://bioinformaticsonline.com/pages/view/36398/tools-for-protein-protein-docking</link>
	<title><![CDATA[Tools for Protein-Protein Docking !]]></title>
	<description><![CDATA[<p>Predicting the structure of protein&ndash;protein complexes using docking approaches is a difficult problem whose major challenges include identifying correct solutions, and properly dealing with molecular flexibility and conformational changes. Following are the tools to predict&nbsp;<span>the structure of protein&ndash;protein complexes:</span></p><p><a href="http://www.sbg.bio.ic.ac.uk/docking/index.html" target="_blank">3D-Dock Suite</a></p><p>Global rigid search: FFTShape complementarity and electrostatics</p><p>Re-scoring and clustering. Refinement of interface side-chains</p><p><a href="http://www.sbg.bio.ic.ac.uk/~3dgarden/" target="_blank">3D-Garden</a></p><p>Global rigid search in ensamble</p><p>Shape complementarity and Lennard&ndash;Jones potential</p><p>Side chain and backbone dihedral refinement</p><p><a href="http://www.sdsc.edu/CCMS/DOT/" target="_blank">DOT</a></p><p>Global rigid search: FFTShape complementarity, electrostatics and VDWNone</p><p><a href="http://users.unimi.it/~ddl/escherng/index.htm" target="_blank">Escher NG</a></p><p>Global rigid searchShape complementarity, hydrogen bonds and electrostatic</p><p>Integrated in&nbsp;<a href="http://users.unimi.it/~ddl/vega/download.htm" target="_blank">VEGA</a></p><p><a href="http://vakser.bioinformatics.ku.edu/resources/gramm/gramm1" target="_blank">GRAMM</a>&nbsp;</p><p>Global rigid search: FFT. smooth protein surface representation for soft docking</p><p>Shape complementarity and Lennard-Jones potential</p><p>Clustering of conformations</p><p><a href="http://vakser.bioinformatics.ku.edu/resources/gramm/grammx/" target="_blank">GRAMM-X</a>&nbsp;</p><p>Global rigid search: FFT. smooth protein surface representation for soft docking</p><p>Shape complementarity and Lennard-Jones potentialminimization and re-scoring with multiple filters</p><p><a href="http://www.loria.fr/~ritchied/hex_server/" target="_blank">HEX</a></p><p>Global rigid search: Fourier correlation of spherical harmonics</p><p>Shape complementarity</p><p><a href="http://www.csd.abdn.ac.uk/hex/" target="_blank"></a><a href="http://haddock.chem.uu.nl/Haddock/haddock.php" target="_blank">HADDOCK</a></p><p>Global rigid searchElectrostatic ,VDW and desolvation energy termsMD simulated annealing refinement . Filtering based on external data.&nbsp;</p><p><a href="http://www.molsoft.com/docking.html">ICM</a></p><p>Global rigid search: Monte CarloEmpirical scoring function</p><p>Clustering and selection of conformations. Refinement of interface side-chains and re-scoring</p><p><a href="http://www.weizmann.ac.il/Chemical_Research_Support/molfit/" target="_blank">MolFit&nbsp;</a></p><p>Global rigid search: FFTShape complementarity</p><p>Clustering of good solutions, filtering using&nbsp;<em>a priori&nbsp;</em>information and small, local rigid rotations around selected conformations</p><p><a href="http://bioinfo3d.cs.tau.ac.il/PatchDock/" target="_blank">PatchDock</a></p><p>Global rigid searchShape complementarity and atomic desolvation energy</p><p>Clustering of conformations</p><p><a href="http://inb.bsc.es/gn6/PyDock" target="_blank">PyDock</a></p><p>Global rigid search:FFTShape complementarity</p><p>rescoring by binding electrostatics and desolvation energy</p><p><a href="http://bioinfo3d.cs.tau.ac.il/PatchDock/" target="_blank"></a><a href="http://rosettadock.graylab.jhu.edu/" target="_blank">RosettaDock</a></p><p>Local rigid search: Monte Carlo with low and high resolution structure representation levels</p><p>Different scoring parameters for the different resolutions&nbsp;</p><p><a href="http://zlab.bu.edu/zdock/" target="_blank">ZDOCK</a></p><p>Global rigid search: FFTShape complementarity, desolvation energy, and electrostatics.</p><p>Energy minimization and re-scoringFree for academics</p><p>&nbsp;</p><p>Point to note:</p><p>The proper treatment of flexibility in protein&ndash;protein docking is still an active field of research. You first should analyzed your proteins in order to define their conformational space and then choose the most suitable method for your docking problem.</p>]]></description>
	<dc:creator>Poonam Mahapatra</dc:creator>
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