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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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<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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<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>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:#79baff;">Education</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: #f1b840">In Journals</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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<td style="padding: 5px;"> {{Proteopedia:Featured EDU/{{#expr: {{#time:U}} mod {{Proteopedia:Number of EDU articles}}}}}}</td>
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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_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>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<td>[[Proteopedia:About|About]]</td>
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<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[Who knows]] ...</p>
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<td>[[Help:Contents|Help]]</td>
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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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<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 16:31, 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
Metal-Ligand Nano-Cages

This self-assembling structure has an interior cavity about 32 Å in diameter. It consists of 24 palladium ions, each of which is coordinated by 4 nitrogens, which are part of 48 dipyridylthiophene molecules. Such synthetic nano-spheres can be functionalized to create synthetic receptors and nanoreactors. Potential applications in sensing, catalysis, and drug delivery are being explored.

>>> See more animations and explanation >>>

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 >>>

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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