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<th style="padding: 10px;background-color: #79baff">Education</th>
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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
Coronavirus Spike Protein Membrane Fusion

by Eric Martz
SARS-CoV-2 spike protein "spears" the host membrane with a fusion peptide and drags the virus envelope membrane transmembrane domain close to the host membrane, initiating fusion. This moves the virus RNA genome into the host cell, initiating infection.
>>> Visit this page >>>

About this image
Molecular Sculpture

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

>>> 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
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 >>>

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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