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proline.html
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<!DOCTYPE html>
<html lang="en">
<head>
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<div class="card-header"> Proline </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="hypoxia_inducible_transcription_factor" src="/models/2XUM.glb"></a-asset-item>
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<a-entity gltf-model="#hypoxia_inducible_transcription_factor" animation-mixer position="30 62 -150" rotation="100 0 20"></a-entity>
</a-scene>
<table>
<tr>
<th> Group, </th>
<th> Alien-Protein-code, </th>
<th> Agent, </th>
<th> Formula, </th>
</tr>
<tr>
<td> carboxy group, </td>
<td> PHD,
HIF,
HPHs
</td>
<td> Neutral, </td>
<td>
<a class="jmol" href="https://chemapps.stolaf.edu/jmol/jmol.php?model=%5BO-%5DC%28%3DO%29%5BC%40H%5D%28CCC2%29%5BNH2%2B%5D2" title="Chemical structure of Proline molecule. In Proline compound Hydrogen atoms are abudant">
C<small class="subscript">5-</small>H<small class="subscript">9-</small>NO<small class="subscript">2</small></td>
</a>
</tr>
<tr>
<th> Weight, </th>
<th> Nature, </th>
<th> Role, </th>
<th> Sidechain, </th>
</tr>
<tr>
<td>
115.132 g·mol−1,
</td>
<td>
Aliphatic,
</td>
<td>
L-Proline has been found to act as a weak agonist of the glycine receptor and of both NMDA and non-NMDA (AMPA/kainate) ionotropic glutamate receptors.
Peptide bond formation with incoming Pro-tRNAPro is considerably slower than with any other tRNAs, which is a general feature of N-alkylamino acids.
Peptide bond formation is also slow between an incoming tRNA and a chain ending in proline; with the creation of proline-proline bonds slowest of all.
The exceptional conformational rigidity of proline affects the secondary structure of proteins near a proline residue and may account for proline's higher prevalence in the proteins of thermophilic organisms.
Proline is also commonly found in turns (another kind of secondary structure), and aids in the formation of beta turns.
Multiple prolines and/or hydroxyprolines in a row can create a polyproline helix, the predominant secondary structure in collagen.
scurvy can result from defects in this hydroxylation, e.g., mutations in the enzyme prolyl hydroxylase or lack of the necessary ascorbate (vitamin C) cofactor.
</td>
<td>
α carbon,
</td>
</tr>
</table>
</p>
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