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<div id="issn">'''''ISSN 2310-6301'''''</div>
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<div id="headerOne">As <b>life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure and function of biomacromolecules.</div>
 
<div id="headerTwo"><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>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
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<tr id="mainPageSections"><th class="mainPageSectionA">Selected Research Pages</th>
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<th class="mainPageSectionB">In Journals</th>
<b>Proteopedia</b> presents this information in a user-friendly way as a '''collaborative & free 3D-encyclopedia of proteins & other biomolecules.'''
<th class="mainPageSectionC">Education</th>
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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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[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]] <br>
<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
[[Proteopedia:Video_Guide|Video Guides]] <br>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
[[Who knows]] ...
<p>[[Who knows]] ...</p>
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<p>[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
[[I3DC|About Interactive 3D Complements - '''I3DCs''']] <br>
<p>[[Proteopedia:I3DC|List of I3DCs]]</p>
[[Proteopedia:I3DC|List of I3DCs]] <br>
<p>[[How to get an I3DC for your paper]]</p>
[[How to get an I3DC for your paper]]
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<p>[[Teaching strategies using Proteopedia]]</p>
[[Teaching strategies using Proteopedia]] <br>
<p>[[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages|Examples of pages for teaching]]</p>
[[Teaching_Scenes%2C_Tutorials%2C_and_Educators%27_Pages|Examples of pages for teaching]] <br>
<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]
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<td>[[Proteopedia:About|About]]</td>
<td>[[Proteopedia:About|About]]</td>
<td>[[Special:Contact|Contact]]</td>
<td>[[Special:Contact|Contact]]</td>
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<td>[[Proteopedia:Structure Index|Structure Index]]</td>
<td>[[Proteopedia:Structure Index|Structure Index]]</td>
<td>[[Help:Contents|Help]]</td>
<td>[[Help:Contents|Help]]</td>
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Latest revision as of 15:44, 16 February 2026

ISSN 2310-6301
As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure and 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

Lifecycle of SARS-CoV-2

What happens if a SARS-CoV-2 coronavirus enters your lung? This molecular animation visualises how the virus particle can take over the host cell and turns it into a virus factory. Eventually, the host cell produces so many viral particles that it dies and releases numerous new virus particles. >>> Visit this page >>>

Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.

IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

>>> Visit this I3DC complement >>>

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

Proteopedia Page Contributors and Editors (what is this?)

Jaime Prilusky, Joel L. Sussman, Angel Herraez