We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

Sandbox Home

From Proteopedia

Revision as of 16:09, 30 September 2025 by Joel L. Sussman (Talk | contribs)

(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)

Jump to: navigation, search

table id="tableColumnsMainPage" style="width:100%;border:2px solid #ddd;border-collapse: collapse;table-layout: fixed; "> <tr><td colspan='3' style="background:#F5F5FC;border:1px solid #ddd;">

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.

</td></tr>

<tr> <th style="padding: 10px;background-color: #33ff7b">Selected Research Pages</th> <th style="padding: 10px;background-color: #f1b840">In Journals</th> <th style="padding: 10px;background-color: #79baff">Education</th> </tr>

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 >>>

</td> <td style="padding: 5px;">

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 >>>

</td> <td style="padding: 5px;">

Make Your Own Electrostatic Potential Maps

Positive (+) and Negative (-) charges on the surface of a protein molecule play crucial roles in its interactions with other molecules, and hence in its functions. Electrostatic potential maps coloring the surface of a protein molecule are a popular way to visualize the distribution of surface charges. Easy to use free software is available to to create these surface maps. Above is an integral membrane potassium channel protein. One of its 4 identical chains is removed so you can see the Negative (-) protein surface contacting the 3 K+ ions.

>>> See Examples and Get Instructions >>>

</td>

</tr>

How to add content to Proteopedia

Video Guides

Who knows ...

</td>

About Interactive 3D Complements - I3DCs

List of I3DCs

How to get an I3DC for your paper

</td>

Teaching strategies using Proteopedia