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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>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>
<p>[[Proteopedia:Video_Guide|Video Guides]]</p>

Revision as of 10:01, 21 October 2018

ISSN 2310-6301

As life is more than 2D, Proteopedia helps to bridge the 3D relationships between function & structure of biomacromolecules


Selected Pages Art on Science 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 >>>

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Molecular Sculpture

by Eric Martz
A historical review on sculptures and physical models of macromolecules.

>>> Visit this page >>>

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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.

>>> Visit this I3DC complement >>>

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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 ...

List of Art on Science pages

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 Table of Contents Structure Index Help

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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