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<p style="margin:0">[[I3DC|About Interactive 3D Complements - '''I3DCs''']]</p>
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<p>[[Help:Contents#For_authors:_contributing_content|How to add content to Proteopedia]]</p>
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<p style="margin:0">[[Proteopedia:I3DC|List of I3DCs]]</p>
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<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
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<p>[[I3DC|About Interactive 3D Complements - '''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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Revision as of 15:48, 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
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Coronavirus Spike Protein Priming

by Eric Martz
Coronavirus SARS-CoV-2 (responsible for COVID-19) has a spike protein on its surface, which enables it to infect host cells. Initially, proteases in the lungs clip the homo-trimeric spike protein at a unique sequence. This primes it, causing it to extend its receptor binding surface (shown in the above animation), optimizing binding to the host cell's ACE2 receptor (not shown). Next, spike protein initiates fusion of the virus and host cell membranes (not shown), enabling the virus RNA to enter the cell and initiate production of new virions. Knowledge of spike protein's molecular structure and function is crucial to developing effective therapies and vaccines.
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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.

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Virus Capsid Geometry

The Capsid of a virus is its outer shell or "skin". Viruses have evolved intricate and elegant ways to assemble capsid protein chains into complete, usually spherical capsids, often with icosahedral symmetry. Pictured is an extremely simplified model of a capsid, where a single enlarged atom represents each of the 360 protein chains in the capsid of the Simian Virus 40 (SV40), a member of a group of cancer-causing viruses that has been extensively researched for decades.

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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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