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<td style="padding: 10px;background-color: #33ff7b">Other Selected Pages</td>
<td style="padding: 10px;background-color: #33ff7b">[[:Category:Featured in Education|Other Selected Pages]]</td>
<td style="padding: 10px;background-color: #dae4d9">More Art on Science</td>
<td style="padding: 10px;background-color: #dae4d9">[[:Category:Featured in Education|More Art on Science]]</td>
<td style="padding: 10px;background-color: #f1b840">Other Journals</td>
<td style="padding: 10px;background-color: #f1b840">[[:Category:Featured in Education|Other Journals]]</td>
<td style="padding: 10px;background-color: #79baff">More on Education</td>
<td style="padding: 10px;background-color: #79baff">[[:Category:Featured in Education|More on Education]]</td>
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Revision as of 13:21, 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
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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Molecular Sculpture

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

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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.

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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.

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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?)

Jaime Prilusky, Joel L. Sussman, Angel Herraez