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<span style="border:none; margin:0; padding:0.3em; color:#000; font-style: italic; font-size: 1.4em;">
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<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
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<b>Proteopedia</b> presents this information in a user-friendly way as a '''collaborative & free 3D-encyclopedia of proteins & other biomolecules.'''
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<div style="position:relative; top:0.2em; font-size:1.2em; padding:5px 5px 5px 10px; float:right;"><b><i>ISSN 2310-6301</i></b></div>
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'''''ISSN 2310-6301'''''
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<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure &amp; function of biomacromolecules
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</span>
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<span style="display:block; margin:0; padding:0.3em; color:#000; font-style:italic; font-size:1.1em; max-width:80%;">
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<b>Proteopedia</b> presents this information in a user-friendly way as a <b>collaborative &amp; free 3D-encyclopedia of proteins &amp; other biomolecules.</b>
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<th style="padding:10px; background-color:#33ff7b;">Selected Research Pages</th>
<th style="padding:10px; background-color:#33ff7b;">Selected Research Pages</th>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[Who knows]] ...</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[Proteopedia:I3DC|List of I3DCs]]</p>
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<p>[[Who knows]] ...</p>
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<p>[[How to get an I3DC for your paper]]</p>
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{{Proteopedia:Featured JRN/{{#expr: {{#time:U}} mod {{Proteopedia:Number of JRN articles}}}}}}
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<p>[[Proteopedia:I3DC|List of I3DCs]]</p>
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<p>[[How to get an I3DC for your paper]]</p>
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<p>[[Teaching strategies using Proteopedia]]</p>
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<p>[[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages|Examples of pages for teaching]]</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p>[[Teaching strategies using Proteopedia]]</p>
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<p>[[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages|Examples of pages for teaching]]</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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{{Proteopedia:Featured EDU/{{#expr: {{#time:U}} mod {{Proteopedia:Number of EDU articles}}}}}}
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Current revision

   <img src="ProteopediaLogo.png" alt="Proteopedia logo" style="height:80px;">
   
     As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
   
   
Proteopedia presents this information in a user-friendly way as a collaborative & free 3D-encyclopedia of proteins & other biomolecules.
       ISSN 2310-6301
Selected Research Pages In Journals Education
About this image
Mutations in Coronavirus Spike Protein

by Eric Martz
Black spots are mutations of concern in SARS-CoV-2 spike protein reported by UK scientists in December, 2020. RNA viruses mutate quickly so mutations are expected. These mutations may speed up contagion, but are unlikely to cause more severe COVID-19 and unlikely to reduce vaccine effectiveness. ACE2 binding residues. Animation shows priming via cleavage by furin.
>>> Visit this page >>>

About this image
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> Visit this I3DC complement >>>

About this image
Touch-Sensitive Channel

Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions.

>>> See more animations and explanation >>>

How to add content to Proteopedia

Video Guides

Who knows ...

About Interactive 3D Complements - I3DCs

List of I3DCs

How to get an I3DC for your paper

Teaching strategies using Proteopedia

Examples of pages for teaching

How to add content to Proteopedia

About Contact Hot News Table of Contents Structure Index Help
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