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| - | <h1>Part:BBa_K1317001 : CDS for resilin-like polypeptide (RLP)</h1>
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| - | <p>
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| - | This part is the coding sequence for the resilin like polypeptide. This sequence was assembled from a consensus of the proresilin exon 1 from Drosophila melanogaster. This protein, in insects, allows resistance and elasticity used for jumping, flapping... The synthetic gene encodes a synthetic protein "resilin-like". The repeated aminoacids allow to retrieve these properties of resistance, resilience and elasticity, but with a minimal pattern of the original protein, which is more suited for downstream applications. It can be used to produce wire presenting these properties after wet-spinning.</p>
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| - | <h3>Sequence and Features</h3>
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| - | <center><img class="modeling" src="https://static.igem.org/mediawiki/2014/5/58/Bdx2014_Part1.png" alt=""/><br><br></center>
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| - | <h3>Design Notes</h3>
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| - | <p>
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| - | The gene used to assemble the biobrick has been provided by GenScript even if the assembling strategy succeeded
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| - | It allows us to have the proper sequence without mutation and with sequencing results.<br>
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| - | The strategy of our assembly is described below anyway. The gene was synthesized by ordering specific oligo with overlapping regions, and by adding a NheI site for further fusing proteins.<br>
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| - | We used the pro-resilin exon 1 from Drosophila melanogaster. We identified a repetitive pattern, PSXXYGAP. So we blast it against the protein database of pro-resilin to check if the pattern was conserved within different species or specific to <i>Drosophila</i>.
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| - | </p>
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| - | <center><img class="" src="https://static.igem.org/mediawiki/parts/d/da/Bdx2014_RLPsynthesis1.png" alt=""/><br><br></center>
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| - | <p>
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| - | We have taken XX randomly and we brought out conserved pattern so we used it to do our resilin like polypeptide with the following pattern: (RLP)<strong> MW-[(PSSSYGAP)(PSNSYGAP)(PSTSYGAP)(PVAYGAP)]3</strong> <br><br>
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| - | The literature delivers some mechanical properties concerning native resilin as high resilience (<90%) that allows the protein to recover its initial folding after a high tensile stress. Thus it can be an interesting characteristic to show and use, so we wanted to test it on our RLP.<br><br>
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| - | <h3>Source</h3>
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| - | <p>
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| - | Genomic sequence from Drosophila melanogaster</p>
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| - | <h3>References</h3>
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| - | <p>
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| - | [1] Tamburro A.M. et al. <i> Molecular and supramolecular structural studies on significant repetitive sequences of resilin</i> (2010) Chembiochem., 11(1), 83-93. doi: 10.1002/cbic.200900460.<br>
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| - | [2] Linqing Li et Kristi L. Kiick.<i> Resilin-Based Materials for Biomedical Applications </i>(2013) ACS Macro Lett., 2(8), 635–640. doi: 10.1021/mz4002194.<br>
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| - | [3] David H. Ardell and Svend Olav Andersen <i>Tentative identification of a resilin gene in Drosophila melanogaster</i> Insect Biochemistry and Molecular Biology 31 (2001) 965–970<br>
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| - | [4] Julie N. Renner et al. <i> Characterization of Resilin-Based Materials for Tissue Engineering Applications Biomacromolecules </i> 2012, 13, 3678−3685<br>
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| - | [5] Russell E. Lyons et al. <i>Comparisons of Recombinant Resilin-like Proteins: Repetitive Domains Are Sufficient to Confer Resilin-like Properties Biomacromolecules </i> 2009, 10, 3009–3014<br>
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| - | [6] M. Kim et al. High yield expression of recombinant pro-resilin: <i>Lactose-induced fermentation in E. coli and facile purification Protein Expression and Purification </i>52 (2007) 230–236<br>
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| - | [7] Christopher M. Elvin et al.<i> Synthesis and properties of crosslinked recombinant pro-resilin</i> Vol 437|13 October 2005|doi:10.1038/nature04085<br><br><br></p>
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| - | </html>
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| | {{:Team:Bordeaux/Pied}} | | {{:Team:Bordeaux/Pied}} |
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