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<b><i>ISSN 2310-6301</i></b>
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<b><i>ISSN 2310-6301</i></b>
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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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<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 '''collaborative &amp; free 3D-encyclopedia of proteins &amp; other biomolecules.'''
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<b>Proteopedia</b> presents this information in a user-friendly way as a '''collaborative &amp; free 3D-encyclopedia of proteins &amp; other biomolecules.'''
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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:#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:#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:#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>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[Proteopedia:I3DC|List of I3DCs]]</p>
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<p>[[Who knows]] ...</p>
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<p>[[How to get an I3DC for your paper]]</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 style="padding:10px;">
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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:About|About]]</td>
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<td>[[Proteopedia:Table of Contents|Table of Contents]]</td>
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<td>[[Special:Contact|Contact]]</td>
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<td>[[Proteopedia:Structure Index|Structure Index]]</td>
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<td>[[Template:MainPageNews|Hot News]]</td>
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<td>[[Help:Contents|Help]]</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 16:20, 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
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 >>>

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
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

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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