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<div style="top:+0.2em; font-size:1.2em; padding:5px 5px 5px 10px; float:right;">'''''ISSN 2310-6301'''''</div>
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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><i>ISSN 2310-6301</i></b>
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<span style="border:none; margin:0; padding:0.3em; color:#000; font-style: italic; font-size: 1.1em;max-width:80%;display:block;">
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<span style="display:block; margin:0; padding:0.3em; color:#000; font-style:italic; font-size:1.4em;">
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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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<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 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>
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<th style="padding: 10px;background-color: #f1b840">In Journals</th>
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<th style="padding:10px; background-color:#33ff7b;">Selected Research Pages</th>
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<th style="padding: 10px;background-color: #79baff">Education</th>
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<th style="padding:10px; background-color:#f1b840;">In Journals</th>
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<th style="padding:10px; background-color:#79baff;">Education</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>[[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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{{Proteopedia:Featured EDU/{{#expr: {{#time:U}} mod {{Proteopedia:Number of EDU articles}}}}}}
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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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<td>[[Proteopedia:About|About]]</td>
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<td>[[Special:Contact|Contact]]</td>
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<td>[[Template:MainPageNews|Hot News]]</td>
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<td>[[Proteopedia:Table of Contents|Table of Contents]]</td>
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<td>[[Proteopedia:Structure Index|Structure Index]]</td>
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<p>[[Proteopedia:I3DC|List of I3DCs]]</p>
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<td>[[Help:Contents|Help]]</td>
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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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<table width='100%' style="padding: 10px; background-color: #d7d8f9; font-size: 1.5em;"><tr>
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<td>[[Proteopedia:About|About]]</td>
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<td>[[Special:Contact|Contact]]</td>
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<td>[[Template:MainPageNews|Hot News]]</td>
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<td>[[Proteopedia:Table of Contents|Table of Contents]]</td>
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<td>[[Proteopedia:Structure Index|Structure Index]]</td>
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<td>[[Help:Contents|Help]]</td>
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Revision as of 16:13, 30 September 2025

       ISSN 2310-6301

     
       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.
Selected Research Pages In Journals Education
About this image
HIV-1 protease

by David Canner
The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water.

>>> 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
Make Your Own Electrostatic Potential Maps

Positive (+) and Negative (-) charges on the surface of a protein molecule play crucial roles in its interactions with other molecules, and hence in its functions. Electrostatic potential maps coloring the surface of a protein molecule are a popular way to visualize the distribution of surface charges. Easy to use free software is available to to create these surface maps. Above is an integral membrane potassium channel protein. One of its 4 identical chains is removed so you can see the Negative (-) protein surface contacting the 3 K+ ions.

>>> See Examples and Get Instructions >>>

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