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<th style="padding: 10px;background-color: #33ff7b">Selected Pages</th>
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<th style="padding: 10px;background-color: #79baff">Education</th>
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<td style="padding: 5px;"> {{Proteopedia:Featured SEL/{{#expr: {{#time:U}} mod {{Proteopedia:Number of SEL articles}}}}}}</td>
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<td style="padding: 10px;background-color: #33ff7b">Other Selected Pages</td>
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<td style="padding: 10px;background-color: #dae4d9">More Art on Science</td>
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<td style="padding: 10px;background-color: #f1b840">Other Journals</td>
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<td style="padding: 10px;background-color: #79baff">More on Education</td>
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<td style="padding: 10px;>How to author pages and contribute to Proteopedia</td>
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<td style="padding: 10px;>How to get an Interactive 3D Complement for your paper</td>
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<td style="padding: 10px;>How to author pages and contribute to Proteopedia</td>
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Revision as of 12:54, 18 October 2018

Because life has more than 2D, Proteopedia helps to understand relationships between structure and function. Proteopedia is a free, collaborative 3D-encyclopedia of proteins & other molecules. ISSN 2310-6301

Selected Pages Art on Science Journals Education
About this image
Mutations in Coronavirus Spike Protein

by Eric Martz
Black spots are mutations of concern in SARS-CoV-2 spike protein reported by UK scientists in December, 2020. RNA viruses mutate quickly so mutations are expected. These mutations may speed up contagion, but are unlikely to cause more severe COVID-19 and unlikely to reduce vaccine effectiveness. ACE2 binding residues. Animation shows priming via cleavage by furin.
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About this image
Opening a Gate to Human Health

by Alice Clark (PDBe)
In the 1970s, an exciting discovery of a family of medicines was made by the Japanese scientist Satoshi Ōmura. One of these molecules, ivermectin, is shown in this artwork bound in the ligand binding pocket of the Farnesoid X receptor, a protein which helps regulate cholesterol in humans. This structure showed that ivermectin induced transcriptional activity of FXR and could be used to regulate metabolism.

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About this image
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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About this image
Transport of Drugs & Nutrients

Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

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Other Selected Pages More Art on Science Other Journals More on Education
How to author pages and contribute to Proteopedia How to get an Interactive 3D Complement for your paper How to author pages and contribute to Proteopedia

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

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