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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>


      <span style="display:block; margin:0; padding:0.3em; color:#000; font-style:italic; font-size:1.4em;">
        <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 <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:#f1b840;">In Journals</th>
    <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>
        <p>[[Proteopedia:Video_Guide|Video Guides]]</p>
        <p>[[Who knows]] ...</p>
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        <p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
        <p>[[Proteopedia:I3DC|List of I3DCs]]</p>
        <p>[[How to get an I3DC for your paper]]</p>
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        <p>[[Teaching strategies using Proteopedia]]</p>
        <p>[[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages|Examples of pages for teaching]]</p>
        <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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          <td>[[Proteopedia:About|About]]</td>
          <td>[[Special:Contact|Contact]]</td>
          <td>[[Template:MainPageNews|Hot News]]</td>
          <td>[[Proteopedia:Table of Contents|Table of Contents]]</td>
          <td>[[Proteopedia:Structure Index|Structure Index]]</td>
          <td>[[Help:Contents|Help]]</td>
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Revision as of 15:57, 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
Avian Influenza Neuraminidase

Eric Martz
The first new influenza virus to emerge as an imminent pandemic threat in the 21st century is H1N1 swine flu. The drug oseltamivir (Tamiflu®) inhibits flu neuraminidase, a component necessary for virus spread, in susceptible flu strains. The development of oseltamivir was guided, in part, by crystallographically determined structures of flu neuraminidase, which is a homotetramer, shown with oseltamivir bound. Oseltamivir was designed to fit N2/N9 (neuraminidases from other strains of flu). Serendipitously, it also fits N1 by induced fit.

>>> Visit this page >>>

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 >>>

You Are What You Eat!

Above is an integral membrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (top) opens and binds peptide or drug (small solid object in the center), then closes, while its cytoplasmic face (bottom) opens to release its cargo into the intestinal cell, which passes it on to the blood circulation.

>>> See more animations and explanation >>>

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