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asparagine.html
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<!DOCTYPE html>
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<div class="card-header"> Asparagine </div>
<div class="card-body">
<h5 class="card-title"> <i class="fa fa-info-circle" aria-hidden="true" title="information about amino-acid"></i>
</h5>
<p class="card-text">
<a-scene>
<a-assets>
<a-asset-item id="FOXO4" src="/models/1E17.glb"></a-asset-item>
</a-assets>
<a-entity gltf-model="#FOXO4" animation-mixer position="20 10 -70"></a-entity>
</a-scene>
<table>
<tr>
<th> Group, </th>
<th> Alien-Protein-code, </th>
<th> Agent, </th>
<th> Formula, </th>
</tr>
<tr>
<td> α-amino acid, and α-carboxylic-acid group </td>
<td> PHD, VHL, OS-9, SSAT2,
RACK1, SSAT1, GSK3β, and FOXO4 </td>
<td> Neutral, </td>
<td>
<a class="jmol" href="https://chemapps.stolaf.edu/jmol/jmol.php?model=C%28%5BC%40%40H%5D%28C%28%3DO%29%5BO-%5D%29%5BNH3%2B%5D%29C%28%3DO%29N" title="Chemical structure of asparagine molecule. Asparagine belong to Carboxamide. In Asparagine compound Hydrogen atoms are abudant.">
C<small class="subscript">4-</small>H<small class="subscript">8-</small>N<small class="subscript">2-</small>O<small>3</small>
</a>
</td>
</tr>
<tr>
<th> Weight, </th>
<th> Nature, </th>
<th> Role, </th>
<th> Sidechain, </th>
</tr>
<tr>
<td>
132.119 g·mol−1,
</td>
<td>
Polar (at pH) & Aliphatic,
</td>
<td>
Asparagine residues are often found near the beginning of alpha-helices as asx turns and asx motifs, and in similar turn motifs, or as amide rings, in beta sheets.
Its role can be thought as "capping" the hydrogen bond interactions that would otherwise be satisfied by the polypeptide backbone.
Asparagine also provides key sites for N-linked glycosylation, modification of the protein chain with the addition of carbohydrate chains.
Asparagine can be hydroxylated in the HIF1 hypoxia inducible transcription factor. This modification inhibits HIF1-mediated gene activation.
Asparagine is required for development and function of the brain.
The availability of asparagine is also important for protein synthesis during replication of poxviruses.
The addition of N-acetylglucosamine to asparagine is performed by oligosaccharyltransferase enzymes in the endoplasmic reticulum.
This glycosylation is important both for protein structure and protein function.
a study found that decreasing levels of asparagine "dramatically" reduced the spread of breast cancer in laboratory mice.
</td>
<td>
Carboxamide,
</td>
</tr>
</table>
</p>
</div>
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