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<div style="top:+0.2em; font-size:1.2em; padding:5px 5px 5px 10px; float:right;">'''''ISSN 2310-6301'''''</div>
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<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
<b>As life is more than 2D</b>, Proteopedia helps to bridge the gap between 3D structure & function of biomacromolecules
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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.
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Revision as of 11:17, 21 October 2018

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. </td></tr>
ISSN 2310-6301

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

Selected Pages Art on Science Journals Education
About this image
The ribosome

by Wayne Decatur
The 2009 Nobel Prize in Chemistry was awarded for studies of the ribosome. The ribosome is the machine in your cells that accurately and efficiently decodes the genetic information stored in your genome and synthesizes the corresponding polypeptide chain one amino acid at a time in the process of translation. These structures are considered landmarks for the fact they showed clearly the major contributions to decoding and peptide bond synthesis come from RNA and not protein, as well as for the sheer size of the structures determined.

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Molecular Sculpture

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

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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.

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About this image
Transport of Drugs & Nutrients

Above is a transmembrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (shown above) opens and binds peptide or drug, then closes, while its cytoplasmic face (opposite end from the above) opens to release its cargo into the intestinal cell, which passes it on into the blood circulation.

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