This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Main Page

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
<span style="border:none; margin:0; padding:0.3em; color:#000; font-style: italic; font-size: 1.1em;max-width:80%;display:block;">
<span style="border:none; margin:0; padding:0.3em; color:#000; font-style: italic; font-size: 1.1em;max-width:80%;display:block;">
-
Often it is difficult to utilize the wealth of information found in 3D biomacromolecular structures. Proteopedia's goal is to present structure/function information on these molecules in a user-friendly manner to a broad scientific audience.
+
Proteopedia's goal is to present structure/function information on 3D biomacromolecules in a user-friendly manner to a broad scientific audience.
</span>
</span>

Revision as of 09:02, 20 January 2019

ISSN 2310-6301

As life is more than 2D, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules

Proteopedia's goal is to present structure/function information on 3D biomacromolecules in a user-friendly manner to a broad scientific audience.


Selected Pages Journals Education

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 >>>

About this image
Structural flexibility of the periplasmic protein, FlgA, regulates flagellar P-ring assembly in Salmonella enterica.

H Matsunami, YH Yoon, VA Meshcheryakov, K Namba, FA Samatey. Scientific Reports 2016 doi: 10.1038/srep27399
A periplasmic flagellar chaperone protein, FlgA, is required for P-ring assembly in bacterial flagella of taxa such as Salmonella enterica or Escherichia coli. Here we present the open and closed crystal structures of FlgA from Salmonella enterica serovar Typhimurium, grown under different crystallization conditions. An intramolecular disulfide cross-linked form of FlgA caused a dominant negative effect on motility of the wild-type strain.

>>> 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 >>>

How to add content to Proteopedia

Video Guides

Who knows ...

About Interactive 3D Complements - I3DCs

List of I3DCs

How to get an I3DC for your paper

Teaching strategies using Proteopedia

Examples of pages for teaching

How to add content to Proteopedia

About Contact Table of Contents Structure Index Help

Proteopedia Page Contributors and Editors (what is this?)

Joel L. Sussman, Jaime Prilusky

Personal tools