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<span style="font-size:2.0em; border:none; margin:0; padding:0.3em; color:#000; font-weight: bold;">Welcome to Proteopedia</span><br>
<span style="font-size:2.0em; border:none; margin:0; padding:0.3em; color:#000; font-weight: bold;">Welcome to Proteopedia</span><br>

Revision as of 07:23, 18 October 2018

Welcome to Proteopedia
ISSN 2310-6301 The free, collaborative 3D-encyclopedia of proteins & other molecules

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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.

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Molecular Sculpture

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

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Coronavirus COVID-19

A novel coronavirus was found to be the cause of a respiratory illness first detected in Wuhan, China in 2019. 3D structural studies are aiding scientists to understand how the coronavirus infects humans and helping to find new ways to treat the viral spread (video by Fusion Animation).

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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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Jaime Prilusky

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