Difference between revisions of "Part:BBa K1974030"
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<h1>'''Modifying and Improving the Existed Biobrick'''</h1> | <h1>'''Modifying and Improving the Existed Biobrick'''</h1> | ||
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− | <b> | + | <b>Previous linker : |
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<html><a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K416001">BBa_K416001</a></html> | <html><a href="https://parts.igem.org/wiki/index.php?title=Part:BBa_K416001">BBa_K416001</a></html> | ||
of 2010 iGEM10_NYU</b> | of 2010 iGEM10_NYU</b> | ||
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GS Linker(BBa_K416001) is a 15 amino acid flexible peptide linker protein domain that is useful for creating functional fusion proteins. So we want to use it to concent the spider toxin peptide and snowdrop lectin. | GS Linker(BBa_K416001) is a 15 amino acid flexible peptide linker protein domain that is useful for creating functional fusion proteins. So we want to use it to concent the spider toxin peptide and snowdrop lectin. | ||
Revision as of 09:04, 21 October 2016
GS linker
Introduction
The GS Linker(BBa_K1974030) that we provided is a 18 amino acid. It is useful for expressing functional fusion proteins. So, we wanted to use it to concent the spider toxin peptide and snowdrop lectin.
Modifying and Improving the Existed Biobrick
Previous linker :
BBa_K416001
of 2010 iGEM10_NYU
GS Linker(BBa_K416001) is a 15 amino acid flexible peptide linker protein domain that is useful for creating functional fusion proteins. So we want to use it to concent the spider toxin peptide and snowdrop lectin.
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. Futrhermore, we found no result in the previous history using the Flexible Peptide GS Linker(BBa_K416001) from 2010 NYU iGEM team. Therefore, we modified the sequence and added three more amino acids from into the linker. In the result, our improved GS Linker is completely proved by our experiments.
Result and Experiment
In the experiment, 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(see Result), 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.
More application of this part
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]