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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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<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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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p>[[Who knows]] ...</p>
<p>[[Who knows]] ...</p>
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<p>[[How to get an I3DC for your paper]]</p>
<p>[[How to get an I3DC for your paper]]</p>
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<p>[[Teaching strategies using Proteopedia]]</p>
<p>[[Teaching strategies using Proteopedia]]</p>

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
Bacteria float with nano-balloons.

ST Huber, D Terwiel, WH Evers, D Maresca, AJ Jakobi. Preprint 2022 doi: 10.1101/2022.05.08.489936
Many kinds of bacteria and archaea control their buoyancy to move to optimal positions in liquid environments. They do this by making nano-compartments called "gas vesicles", long "pipes" with closed ends filled with gases. In 2022, gas vesicle structure was solved, revealing self-assembling thin-walled cylinders of remarkable strength with gas-permeable pores and water-repelling (hydrophobic) interiors. Building on this structural knowledge, gas vesicles are being engineered to serve as biosensors that report via ultrasound.

>>> Visit I3DC Interactive Visualizations >>>

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
Tutorial: The Ramachandran principle, phi (φ) and psi (ψ) angles in proteins

by Eric Martz
The Ramachandran Principle says that alpha helices, beta strands, and turns are the most likely conformations for a polypeptide chain to adopt, because most other conformations are impossible due to steric collisions between atoms. Check Show Clashes to see where non-bonded atoms are overlapping, and thus in physically impossible positions.

>>> Visit this tutorial >>>

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

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