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<b>Because life has more than 2D</b>, Proteopedia helps to understand relationships between structure and function. <b>Proteopedia</b> is a free, collaborative 3D-encyclopedia of proteins & other molecules.</span>
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<b>Because life has more than 2D</b>, Because life is more than 2D, Proteopedia aids in understanding the 3D relationships between function & structure of biomacromolecules
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Revision as of 07:46, 21 October 2018

ISSN 2310-6301

Because life has more than 2D, Because life is more than 2D, Proteopedia aids in understanding the 3D relationships between function & structure of biomacromolecules


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Coronavirus Spike Protein Membrane Fusion

by Eric Martz
SARS-CoV-2 spike protein "spears" the host membrane with a fusion peptide and drags the virus envelope membrane transmembrane domain close to the host membrane, initiating fusion. This moves the virus RNA genome into the host cell, initiating infection.
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Molecular Sculpture

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

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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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Touch-Sensitive Channel

Touching stretches cell membranes, opening mechanosensitive ion channels, leading to sensation by the nervous system. Pictured is the transmembrane region of a similar channel in bacteria. When closed, the narrow opening is lined by hydrophobic amino acid sidechains, making it non-conductive to ions.

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