Difference between revisions of "Team:Lethbridge/Improve"
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description:Valine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis. | + | <li>Brief Description:Valine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.</li> |
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description: IF1 is a prokaryotic protein that interacts with the ribosome by binding to the A site, preventing aminoacyl tRNA from entering the ribosome. | + | <li>Brief Description: IF1 is a prokaryotic protein that interacts with the ribosome by binding to the A site, preventing aminoacyl tRNA from entering the ribosome.</li> |
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description: IF-3 is a prokaryotic protein that binds to the 30S subunit of the ribosome to increase chances of availability for starting protein synthesis. | + | <li>Brief Description: IF-3 is a prokaryotic protein that binds to the 30S subunit of the ribosome to increase chances of availability for starting protein synthesis.</li> |
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description:EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor which catalyzes the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome for the creation of the peptide chain. | + | <li>Brief Description:EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor which catalyzes the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome for the creation of the peptide chain.</li> |
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<div style="clear: both"></div> | <div style="clear: both"></div> | ||
| − | |||
<div class="oneText-Wrapper"><div class="oneText-Text"> | <div class="oneText-Wrapper"><div class="oneText-Text"> | ||
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description: EF-Ts is a prokaryotic elongation factor. EF-Ts acts at the guanine nucleotide exchange factor for EF-Tu. It releases GTP from EF-Tu, enabling EF-Tu to bind to a new GTP molecule and catalyze another tRNA addition. | + | <li>Brief Description: EF-Ts is a prokaryotic elongation factor. EF-Ts acts at the guanine nucleotide exchange factor for EF-Tu. It releases GTP from EF-Tu, enabling EF-Tu to bind to a new GTP molecule and catalyze another tRNA addition.</li> |
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
| Line 239: | Line 229: | ||
<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief Description: Myokinase (MK) is a phosphotransferase enzyme that is responsible for the catalyzing the interconversion of adenine nucleotides (ATP, ADP, and AMP), which is crucial for energy homeostasis in the cell. | + | <li>Brief Description: Myokinase (MK) is a phosphotransferase enzyme that is responsible for the catalyzing the interconversion of adenine nucleotides (ATP, ADP, and AMP), which is crucial for energy homeostasis in the cell.</li> |
| − | + | ||
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<div class="textImage-Wrapper"> | <div class="textImage-Wrapper"> | ||
<div class="textImage-Text"><h3><a href="http://parts.igem.org/Part:BBa_K2683029" target="_blank" class="f12>Nucleoside Diphosphate Kinase (NDK)</a></h3></div> | <div class="textImage-Text"><h3><a href="http://parts.igem.org/Part:BBa_K2683029" target="_blank" class="f12>Nucleoside Diphosphate Kinase (NDK)</a></h3></div> | ||
| + | <div class="textImage-Image"><center><!--IMAGEGOESHERE--></center> | ||
| + | </div></div> | ||
| + | <div style="clear: both"></div> | ||
<div class="oneText-Wrapper"><div class="oneText-Text"> | <div class="oneText-Wrapper"><div class="oneText-Text"> | ||
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<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief description: NDK is responsible for the exchange of a phosphates between different nucleoside diphosphates (NDP) and triphosphates (NTP). | + | <li>Brief description: NDK is responsible for the exchange of a phosphates between different nucleoside diphosphates (NDP) and triphosphates (NTP).</li> |
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
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<div class="textImage-Wrapper"> | <div class="textImage-Wrapper"> | ||
<div class="textImage-Text"><h3><a href="http://parts.igem.org/Part:BBa_K2683030" target="_blank" class="f12>Peptidyl Prolyl Isomerase (PPiase)</a></h3></div> | <div class="textImage-Text"><h3><a href="http://parts.igem.org/Part:BBa_K2683030" target="_blank" class="f12>Peptidyl Prolyl Isomerase (PPiase)</a></h3></div> | ||
| + | <div class="textImage-Image"><center><!--IMAGEGOESHERE--></center> | ||
| + | </div></div> | ||
| + | <div style="clear: both"></div> | ||
<div class="oneText-Wrapper"><div class="oneText-Text"> | <div class="oneText-Wrapper"><div class="oneText-Text"> | ||
| Line 273: | Line 265: | ||
<li> Submitted by: Lethbridge iGEM 2017</li> | <li> Submitted by: Lethbridge iGEM 2017</li> | ||
<li>Designed by: iGEM17_Lethbridge</li> | <li>Designed by: iGEM17_Lethbridge</li> | ||
| − | <li>Brief description: This protein catalyzes the addition of the proline amino acid onto the peptide chain during protein synthesis. | + | <li>Brief description: This protein catalyzes the addition of the proline amino acid onto the peptide chain during protein synthesis.</li> |
| − | + | ||
| − | </li> | + | |
</ul> | </ul> | ||
</div> | </div> | ||
Revision as of 01:50, 18 October 2018
The following constructs are improved by being cloned and confirmed to be into the pSB1C3 plasmid, thus making them able to express in E. coli and used for iGEM user applications. Our project focuses on encapsulation of cargo by protein nanocompartments. This technology can be used to encapsulate cell free systems. The Next Vivo project, designed by the Lethbridge iGEM team in 2017 is therefore an important and viable application for our toolkit. We hope in the future to try encapsulating this system as an alternative to liposome encapsulation as previously proposed for this project. The ability to target cell types could increase the cell free technology we are still developing.
- Original Part: BBa_K2443029
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief description: Release factor 1 (RF1) works with release factor 2 and 3 to cause the termination of translation by recognizing the stop codon in the mRNA sequence in question.
- Original Part: BBa_K2443030
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: Release factor 2 (RF2) works with release factors 1 and 2 to cause the termination of translation by recognizing the stop codon in the mRNA sequence in question.
- Original Part: BBa_K2443004
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief description: Cysteine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.
- Original Part: BBa_K2443012
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief description: Lysine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.
- Original Part: BBa_K2443014
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: Phenylalanine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis. The alpha subunit is one of the two subunits for this function.
- Original Part: BBa_K2443019
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: Serine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.
- Original Part: BBa_K2443023
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description:Valine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.
- Original Part: BBa_K2443024
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: IF1 is a prokaryotic protein that interacts with the ribosome by binding to the A site, preventing aminoacyl tRNA from entering the ribosome.
- Original Part: BBa_K2443025
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: IF-3 is a prokaryotic protein that binds to the 30S subunit of the ribosome to increase chances of availability for starting protein synthesis.
- Original Part: BBa_K2443027
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description:EF-Tu (elongation factor thermo unstable) is a prokaryotic elongation factor which catalyzes the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome for the creation of the peptide chain.
- Original Part: BBa_K2443028
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: EF-Ts is a prokaryotic elongation factor. EF-Ts acts at the guanine nucleotide exchange factor for EF-Tu. It releases GTP from EF-Tu, enabling EF-Tu to bind to a new GTP molecule and catalyze another tRNA addition.
- Original Part: BBa_K2443033
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief Description: Myokinase (MK) is a phosphotransferase enzyme that is responsible for the catalyzing the interconversion of adenine nucleotides (ATP, ADP, and AMP), which is crucial for energy homeostasis in the cell.
- Original Part: BBa_K2443035
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief description: NDK is responsible for the exchange of a phosphates between different nucleoside diphosphates (NDP) and triphosphates (NTP).
- Original Part: BBa_K2443036
- Submitted by: Lethbridge iGEM 2017
- Designed by: iGEM17_Lethbridge
- Brief description: This protein catalyzes the addition of the proline amino acid onto the peptide chain during protein synthesis.