Difference between revisions of "Team:Lethbridge/Improve"

 
(22 intermediate revisions by 3 users not shown)
Line 5: Line 5:
 
<html>
 
<html>
 
<style>
 
<style>
−
.content a {color: darkslategray !important; text-decoration: underline !important}
+
.content a, .content h1 {color: darkslategray !important; text-decoration: underline !important}
 
</style>
 
</style>
 
<body>
 
<body>
Line 12: Line 12:
 
<div class="content"> <!--everything added for content goes after this line-->
 
<div class="content"> <!--everything added for content goes after this line-->
  
 +
<div class="oneText-Wrapper">
 +
<div class="oneText-Text">
 +
    <p class="f12">The following constructs are improved by being cloned and confirmed to be into the pSB1C3 plasmid, thus making them able to express in <i>E. coli</i> 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 N<i>ex</i>t <i>vivo</i> project, designed by the <a href="https://2017.igem.org/Team:Lethbridge">Lethbridge iGEM team</a> 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. Additionally, we hope that cell-free synthesis of protein nanocompartments can also be accomplished using our N<i>ex</i>t <i>vivo</i> system</p>
 +
</div>
 +
</div>
  
−
    <p class="f12">The following constructs are improved by being cloned and confirmed to be into the pSB1C3 plasmid, thus making them able to express in <i>E. coli</i> 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 <a href="https://2017.igem.org/Team:Lethbridge">Lethbridge iGEM team </a> 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. 
+
<div style="clear: both"></div>
−
</p>
+
 
−
    <h3><a href="http://parts.igem.org/Part:BBa_K2683016" target="_blank">Release Factor 1</a></h3>
+
<div class="textImage-Wrapper">
−
<img src="https://static.igem.org/mediawiki/2018/9/97/T--Lethbridge--RF1.PNG" alt="RF1 construct">
+
<div class="textImage-Text">
−
    <ul style="list-style-type:none">
+
  <h3 id="left"><a href="" target="_blank" class="f12">Release Factor 1</a></div>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443029" target="_blank">BBa_K2443029</a></li>
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/b/bc/T--Lethbridge--RF12018.png" alt="RF1 construct"></center>
 +
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
<ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443029" target="_blank">BBa_K2443029</a>
 
         <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: 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.</li>
 
         <li>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.</li>
−
    </ul>
+
</div></div>
−
 
+
 
−
    <h3><a href="http://parts.igem.org/Part:BBa_K2683017" target="_blank">Release Factor 2</a></h3>
+
<div style="clear: both"></div> 
−
     <ul style="list-style-type:none">
+
 
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443030" target="_blank">BBa_K2443030</a></li>
+
<div class="textImage-Wrapper">
 +
<div class="textImage-Text"><a href="http://parts.igem.org/Part:BBa_K2683017" target="_blank" class="f12">Release Factor 2</a></div>
 +
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/3/3e/T--Lethbridge--RF22018.png"></center>
 +
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443030" target="_blank">BBa_K2443030</a>
 
         <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: 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.</li>
 
         <li>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.</li>
 
     </ul>
 
     </ul>
−
 
+
</div></div>
−
   
+
 
−
      <h3><a href="http://parts.igem.org/Part:BBa_K2683018" target="_blank">Cysteine tRNA Synthetase</a></h3>
+
<div style="clear: both"></div> 
−
     <ul style="list-style-type:none">
+
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443004" target="_blank">BBa_K2443004</a></li>
+
<div class="textImage-Wrapper">
 +
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683018" target="_blank" class="f12">Cysteine tRNA Synthetase</a></h2></div>
 +
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/c/c9/T--Lethbridge--Cys2018.png" /></center>
 +
</div></div>
 +
 
 +
<div style="clear: both"></div>
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443004" target="_blank">BBa_K2443004</a>
 
         <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: Cysteine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.</li>
 
         <li>Brief description: Cysteine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.</li>
 
     </ul>
 
     </ul>
−
   
+
</div>
−
        <h3><a href="http://parts.igem.org/Part:BBa_K2683019" target="_blank">Lysine tRNA Synthetase</a></h3>
+
</div>
−
    <ul style="list-style-type:none">
+
 
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443012" target="_blank">BBa_K2443012</a></li>
+
<div style="clear: both"></div>
 +
 
 +
<div class="textImage-Wrapper">
 +
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683019" target="_blank" class="f12">Lysine tRNA Synthetase</a></h2></div>
 +
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/d/d8/T--Lethbridge--Lys2018.png" /></center>
 +
</div></div>
 +
 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
<ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443012" target="_blank">BBa_K2443012</a>
 
         <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: Lysine tRNA synthetase works in the cell by attaching cysteine onto its tRNA to form an aminoacyl-tRNA for protein synthesis.
+
         <li>Brief description: Lysine 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>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
  <h3><a href="http://parts.igem.org/Part:BBa_K2683020" target="_blank">Phenylalanine tRNA Synthetase alpha subunit (PheRS alpha) </a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683020" target="_blank" class="f12">Phenylalanine tRNA Synthetase alpha subunit (PheRS alpha) </a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/b/b6/T--Lethbridge--Phe2018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443014" target="_blank">BBa_K2443014</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443014" target="_blank">BBa_K2443014</a>
 
         <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>
Line 59: Line 103:
 
</li>
 
</li>
 
     </ul>     
 
     </ul>     
 +
</div>
 +
</div>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683022" target="_blank">Serine tRNA Synthetase (SerRS) </a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683022" target="_blank" class="f12">Serine tRNA Synthetase (SerRS) </a></h2></div>
−
    <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/e/ee/T--Lethbridge--Ser2018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443019" target="_blank">BBa_K2443019</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
<ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443019" target="_blank">BBa_K2443019</a>
 
         <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>
Line 69: Line 122:
 
</li>
 
</li>
 
     </ul>     
 
     </ul>     
 +
</div>
 +
</div>
 +
 +
<div style="clear: both"></div>
 
          
 
          
−
   
+
<div class="textImage-Wrapper">
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683023" target="_blank">Valine tRNA Synthetase (ValRS) </a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683023" target="_blank" class="f12">Valine tRNA Synthetase (ValRS) </a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/8/87/T--Lethbridge--Val2018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443023" target="_blank">BBa_K2443023</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443023" target="_blank">BBa_K2443023</a>
 
         <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>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683024" target="_blank">Initiation Factor I (IF1)</a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683024" target="_blank" class="f12">Initiation Factor I (IF1)</a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/f/fb/T--Lethbridge--IF12018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443024" target="_blank">BBa_K2443024</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443024" target="_blank">BBa_K2443024</a>
 
         <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>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
    <h3><a href="http://parts.igem.org/Part:BBa_K2683025" target="_blank">Initiation Factor 3 (IF1)</a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683025" target="_blank" class="f12">Initiation Factor 3 (IF1)</a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/f/f6/T--Lethbridge--IF32018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443025" target="_blank">BBa_K2443025</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443025" target="_blank">BBa_K2443025</a>
 
         <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>
 +
    </ul>           
 +
</div>
 +
</div>
  
−
</li>
+
<div style="clear: both"></div>
−
    </ul>          
+
−
   
+
 
      
 
      
−
    <h3><a href="http://parts.igem.org/Part:BBa_K2683026" target="_blank">Elongation Factor- Thermo Unstable (EF-Tu) </a></h3>
+
<div class="textImage-Wrapper">
−
     <ul style="list-style-type:none">
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683026" target="_blank" class="f12">Elongation Factor- Thermo Unstable (EF-Tu) </a></h2></div>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443027" target="_blank">BBa_K2443027</a></li>
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/9/90/T--Lethbridge--Eftu.png" /></center>
 +
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443027" target="_blank">BBa_K2443027</a>
 
         <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>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683027" target="_blank">Elongation Factor-Thermo Stable (EF-Ts)</a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683027" target="_blank" class="f12">Elongation Factor-Thermo Stable (EF-Ts)</a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/1/12/T--Lethbridge--Efts.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443028" target="_blank">BBa_K2443028</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div> 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443028" target="_blank">BBa_K2443028</a>
 
         <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>
 +
 +
<div style="clear: both"></div>
 
      
 
      
−
   
+
<div class="textImage-Wrapper">
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683028" target="_blank">MyoKinase (MK)</a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683028" target="_blank" class="f12">MyoKinase (MK)</a></h2></div>
−
<img src="https://static.igem.org/mediawiki/2018/c/ce/T--Lethbridge--MK.PNG" alt="MK construct">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/c/ce/T--Lethbridge--MK.PNG" alt="MK construct"></center>
−
     <ul style="list-style-type:none">
+
</div></div>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443033" target="_blank">BBa_K2443033</a></li>
+
 
 +
<div style="clear: both"></div> 
 +
 
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443033" target="_blank">BBa_K2443033</a>
 
         <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>
 +
    </ul>           
 +
</div>
 +
</div>
  
 +
<div style="clear: both"></div>
  
−
</li>
+
<div class="textImage-Wrapper">
−
    </ul>          
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683029" target="_blank" class="f12">Nucleoside Diphosphate Kinase (NDK)</a></h2></div>
−
   
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/0/0f/T--Lethbridge--NDK2018.png" /></center>
−
<h3><a href="http://parts.igem.org/Part:BBa_K2683029" target="_blank">Nucleoside Diphosphate Kinase (NDK)</a></h3>
+
</div></div>
−
     <ul style="list-style-type:none">
+
 
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443035" target="_blank">BBa_K2443035</a></li>
+
<div style="clear: both"></div>
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443035" target="_blank">BBa_K2443035</a>
 
         <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>
 +
    </ul>           
 +
</div>
 +
</div>
  
−
</li>
+
<div style="clear: both"></div>
−
    </ul>          
+
 
          
 
          
−
   
+
<div class="textImage-Wrapper">
−
    <h3><a href="http://parts.igem.org/Part:BBa_K2683030" target="_blank">Peptidyl Prolyl Isomerase (PPiase)</a></h3>
+
<div class="textImage-Text"><h2><a href="http://parts.igem.org/Part:BBa_K2683030" target="_blank" class="f12">Peptidyl Prolyl Isomerase (PPiase)</a></h2></div>
−
     <ul style="list-style-type:none">
+
<div class="textImage-Image"><center><img src="https://static.igem.org/mediawiki/2018/4/4d/T--Lethbridge--PPiase2018.png" /></center>
−
        <li>Original Part: <a href="http://parts.igem.org/Part:BBa_K2443036" target="_blank">BBa_K2443036</a></li>
+
</div></div>
 +
 
 +
<div style="clear: both"></div>
 +
 
 +
<div class="oneText-Wrapper"><div class="oneText-Text">
 +
     <ul style="list-style-type:none" class="f11" id="left">Original Part: <a href="http://parts.igem.org/Part:BBa_K2443036" target="_blank">BBa_K2443036</a>
 
         <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>
 +
    </ul> 
 +
</div>
 +
</div>
  
−
</li>
+
<div style="clear: both"></div>
−
    </ul>
+
  
 
</div> <!--this closes off the content div-->
 
</div> <!--this closes off the content div-->
 
</body>
 
</body>
 
</html>
 
</html>

Latest revision as of 03:48, 18 October 2018



Improved Parts Banner Image

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. Additionally, we hope that cell-free synthesis of protein nanocompartments can also be accomplished using our Next vivo system

Release Factor 1

RF1 construct
    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.
Release Factor 2
    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.

Cysteine tRNA Synthetase

    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.

Lysine tRNA Synthetase

    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.

Phenylalanine tRNA Synthetase alpha subunit (PheRS alpha)

    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.

Serine tRNA Synthetase (SerRS)

    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.

Valine tRNA Synthetase (ValRS)

    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.

Initiation Factor I (IF1)

    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.

Initiation Factor 3 (IF1)

    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.

Elongation Factor- Thermo Unstable (EF-Tu)

    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.

Elongation Factor-Thermo Stable (EF-Ts)

    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.

MyoKinase (MK)

MK construct
    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.

Nucleoside Diphosphate Kinase (NDK)

    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).

Peptidyl Prolyl Isomerase (PPiase)

    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.