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

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
 +
<style>
 +
#tableColumnsMainPage td { vertical-align: top !important; }
 +
</style>
<table id="tableColumnsMainPage" style="width:100%; border:2px solid #ddd; border-collapse:collapse; table-layout:fixed;">
<table id="tableColumnsMainPage" style="width:100%; border:2px solid #ddd; border-collapse:collapse; table-layout:fixed;">
<!-- HEADER -->
<!-- HEADER -->

Revision as of 16:01, 30 September 2025

<style> 

 #tableColumnsMainPage td { vertical-align: top !important; }

</style>

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.
Selected Research Pages In Journals Education
About this image
HIV-1 protease

by David Canner
The X-ray structure of HIV-1 protease reveals that it is composed of two symmetrically related subunits which form a tunnel where they meet. This is critical because it contains the active site of the protease, consisting on two Asp-Thr-Gly conserved sequences, making it a member of the aspartyl protease family. The two catalytic Asp's either interact with the incoming water or protonate the carbonyl to make the carbon more electrophilic for the incoming water.

>>> 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
2025 Nobel Prize

by Wayne Decatur
The 2025 Nobel Prize in Chemistry was awarded for studies of metal-organic frameworks. Against expectations, the building blocks of metal-organic frameworks turned out to form networks with large cavities and the materials have a wide range of far-reaching practical applications.

>>> Visit this page >>>

About Contact Hot News Table of Contents Structure Index Help
Retrieved from "http://52.214.119.220/wiki/index.php/Sandbox_Home"
Personal tools