TiffanyChien (Talk | contribs) |
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<p class="title">Improvement of Previoius BioBrick</p> | <p class="title">Improvement of Previoius BioBrick</p> | ||
− | <p class="content">This year, we have designed fusion proteins of spider toxin in conjunction with snowdrop lectin by the three-alanine linker. Through the reference searching, we found that the previous research all used the three-alanine linker. In the experiment, we hypothesized that an elongated linker would enhance the function of the fusion protein for the original linker is too short for the proper folding of the two domains. So we went to the linker library in iGEM part registry website to search for a longer linker. At first, we planned to use the Flexible Peptide GS Linker(<a href="http://parts.igem.org/Part:BBa_K416001" style="color:#44E287;">BBa_K416001</a>) from 2010 NYU iGEM team. However, we found no result in the previous history using this linker. Therefore, we modified the sequence and added three more amino acids into the linker in case it was still too short for proper protein folding. In the experiment(See the <a href="#" style="color:#44E287;"> | + | <p class="content">This year, we have designed fusion proteins of spider toxin in conjunction with snowdrop lectin by the three-alanine linker. Through the reference searching, we found that the previous research all used the three-alanine linker. In the experiment, we hypothesized that an elongated linker would enhance the function of the fusion protein for the original linker is too short for the proper folding of the two domains. So we went to the linker library in iGEM part registry website to search for a longer linker. At first, we planned to use the Flexible Peptide GS Linker(<a href="http://parts.igem.org/Part:BBa_K416001" style="color:#44E287;">BBa_K416001</a>) from 2010 NYU iGEM team. However, we found no result in the previous history using this linker. Therefore, we modified the sequence and added three more amino acids into the linker in case it was still too short for proper protein folding. In the experiment(See the <a href="#" style="color:#44E287;">Link</a>), the fusion protein with the elongated GS linker did show the enhanced repellent effect. Observed from the phenomenon, we did prove the enhanced function of the fusion proteins, so we speculate that the fusion protein has a better secondary structure than the original ones. As a result, we have submitted a basic part for the improved elongated GS linker.(See the <a href="#" style="color:#44E287;">Link</a>)</p> |
</div> | </div> | ||
</section> | </section> |
Revision as of 16:04, 17 October 2016