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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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<span style="display:block; 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 &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:#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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<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 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
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
Structure of Anticancer Ruthenium Half-Sandwich Complex Bound to Glycogen Synthase Kinase 3ß

G Atilla-Gocumen, L Di Costanzo, E Meggers. J Biol Inorg Chem. 2010 doi: 10.1007/s00775-010-0699-x
A crystal structure of an organometallic half-sandwich ruthenium complex bound to glycogen synthase kinase 3ß (GSK-3ß) reveals that the inhibitor binds to the ATP binding site via an induced fit mechanism utilizing several hydrogen bonds and hydrophobic interactions. Importantly, the metal is not involved in any direct interaction with the protein kinase but fulfills a purely structural role.

>>> 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 >>>

About Contact Hot News Table of Contents Structure Index Help
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