Difference between revisions of "Team:Franconia/Parts"

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<h1>Parts</h1>
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<p>Each team will make new parts during iGEM and will submit them to the Registry of Standard Biological Parts. The iGEM software provides an easy way to present the parts your team has created. The <code>&lt;groupparts&gt;</code> tag (see below) will generate a table with all of the parts that your team adds to your team sandbox.</p>
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.read-more-content {
<p>Remember that the goal of proper part documentation is to describe and define a part, so that it can be used without needing to refer to the primary literature. Registry users in future years should be able to read your documentation and be able to use the part successfully. Also, you should provide proper references to acknowledge previous authors and to provide for users who wish to know more.</p>
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<h5>Note</h5>
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<h1>Parts</h1>
<p>Note that parts must be documented on the <a href="http://parts.igem.org/Main_Page"> Registry</a>. This page serves to <i>showcase</i> the parts you have made. Future teams and other users and are much more likely to find parts by looking in the Registry than by looking at your team wiki.</p>
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<div class = "content">
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<div class = "row">
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<div class = "col-sm-6">
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<h3>BBa_K2419000</h3>
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<div class = "subtitle"><p>SpyTag-ELP5-SnoopCatcher for elastomeric tissue</p></div>
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<p>This part can be used to form an elastomeric tissue. The elastin like protein ELP5 as the main part has a SpyTag and a SnoopCatcher at its end to be able to bind its counterpart "SnoopTag-ELP5-SpyCatcher". Those two kind of proteins can build long polymer chains which can form an elastomeric tissue i.e. for the application as the basic tissue of artificial muscles.</p>
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</div>
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<div class = "col-sm-6">
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<h3>BBa_K2419002</h3>
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<div class = "subtitle"><p>W51W54 for conductive pili production</p></div>
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<p>This part can be used to express conductive pili of Geobacter Sulfurreducens in E.coli bacteria. Since the cultivation of Geobacter Sulfurreducens is difficult due to its strictly anaerobic demand, the expression of the pili in E.coli is the more convenient. The pili can then be used i.e. as the conductive layers of a dielectrical elastomeric actuator for the application of an artificial muscle.
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</p>
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</div>
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<div class = "row">
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<div class = "col-sm-6">
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<h3>BBa_K2419001</h3>
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<div class = "subtitle"><p>SpyTag-Streptavidin-ELP5-SnoopCatcher for elastomeric tissue connection with molecular machines</p></div>
 +
<p>This part can be used to form an elastomeric tissue. The elastin like protein ELP5 as the main part has a SpyTag and a SnoopCatcher at its end to be able to bind its counterpart "SnoopTag-ELP5-SpyCatcher". Those two kind of proteins can build long polymer chains which can form an elastomeric tissue i.e. for the application as the basic tissue of artificial muscles. Additionally, the part contains a streptavidin tag for binding to i.e. biotin anchored molecular machines. This cross-linking enables the proteins to form an artificial muscle that can contract and relax in its structure by light stimuli through the mole
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cular machines.</p>
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</div>
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<div class = "col-sm-6">
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<h3>BBa_K2419003</h3>
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<div class = "subtitle"><p>TagCFP for analysis of elastomeric tissue</p></div>
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<p>TagCFP is a monomeric protein emitting bright cyan light. It is based on the natural fluorescence of the jellyfish Aequorea macrodactyla, which expresses a GFP-like fluorescent protein. This part can be used to analyze the quality i.e. of an elastomeric tissue out of proteins connected via Catcher-Tag systems (see BBa_K2419000). While such a tissue is formed, TagCFP as a fluorescent protein can be added due to its strong fluorescent emission. As a result, the maxima of emission and absorption of the fluorescent protein shift to a higher level when excited by the specific absorption light wavelength. This shift can only be ascribed to the assembly of TagCFP to the tissue. The behavior of the emission and absorption can therefore be used as a screen of the tissue around the fluorescent protein. The tissue network can be characterized regarding its structure and density. These parameters will give information about the quality of the polymeric network.
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</p>
  
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<div class = "read-more-content">
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<div class = "subtitle"><p>Testing the indicational function of TagCFP in an elastomeric tissue</p></div>
  
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<p>To test the indicational function of TagCFP we created a hydrogel resembling the elastomeric tissue. We then added TagCFP both into water and the hydrogel. The results of this test are shown in Figure 1. On the right, TagCFP fluoresces in a cyan color when added to water and excited with light. Whereas the fluorescence color changes to a light blue when excited with light while being located in the hydrogel.</p>
  
<h5>Adding parts to the registry</h5>
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<div class="center">
<p>You can add parts to the Registry at our <a href="http://parts.igem.org/Add_a_Part_to_the_Registry">Add a Part to the Registry</a> link.</p>
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<img src = "https://static.igem.org/mediawiki/2017/f/f6/T--Franconia--Parts--Parts_1_1.png">
<p>We encourage teams to start completing documentation for their parts on the Registry as soon as you have it available. The sooner you put up your parts, the better you will remember all the details about your parts. Remember, you don't need to send us the DNA sample before you create an entry for a part on the Registry. (However, you <b>do</b> need to send us the DNA sample before the Jamboree. If you don't send us a DNA sample of a part, that part will not be eligible for awards and medal criteria.)</p>
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<div>Figure 1: TagCFP in water (right) and TagCFP in hydrogel (left).</div>
</div>
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</div>
  
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<p>These results visibly show the effect of TagCFP being added to different solutions. The change of the color from cyan in water to light blue in the hydrogel indicates a shift of the emission maximum and therefore TagCFP can be used as a qualitatively test for elastomeric tissue, while additionally, further characterization of the tissue can be achieved.
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Characterization
  
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We further characterized the TagCFP to supply a broader understanding of the properties of this fluorescent protein. We therefore measured the absorption and emission of TagCFP. The regarding graph is given below (Figure 2).
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</p>
  
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<div class="center">
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<img src = "https://static.igem.org/mediawiki/2017/8/81/T--Franconia--Parts--1.2.png">
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<div>Figure 2: Fluorescence spectrum of TagCFP showing absorption and emission at variant wavelengths.</div>
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</div>
  
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<p>The results show a difference in the wavelength of the absorption and the emission. The absorption of TagCFP has its maximum at a wavelength of 457.4 nm and the emission maximum lays at a wavelength of 478.1 nm. The overlap of absorption and emission can be seen in the area around 470 nm.
  
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<br>We further plotted the measured values of the excitation wavelength and the emission wavelength of TagCFP to obtain a height profile given in the diagram below (Figure 3).
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</p>
  
<h5>What information do I need to start putting my parts on the Registry?</h5>
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<div class="center">
<p>The information needed to initially create a part on the Registry is:</p>
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<img src = "https://static.igem.org/mediawiki/2017/c/cf/T--Franconia--Parts--Parts_1_3.png">
<ul>
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<div>Figure 3: Excitation wavelength and emission wavelength of TagCFP.</div>
<li>Part Name</li>
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</div>
<li>Part type</li>
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<p>The diagram displays the distribution of the different wavelengths. The red colored area reveals the overlap of excitation and emission at its uppermost distinctness.
<li>Creator</li>
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</p>
<li>Sequence</li>
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<li>Short Description (60 characters on what the DNA does)</li>
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<button class="read-more">
<li>Long Description (Longer description of what the DNA does)</li>
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        <i class="fa fa-angle-double-down"></i>
<li>Design considerations</li>
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<p>
 
We encourage you to put up <em>much more</em> information as you gather it over the summer. If you have images, plots, characterization data and other information, please also put it up on the part page. </p>
 
  
</div>
 
  
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<h4>Further characterization of EGFP</h4>
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<p>We further characterized the “EGFP Protein Production Construct” (Part:BBa_K1123005) of the group iGEM13_TU-Eindhoven to supply a broader understanding of the properties of this fluorescent protein. We therefore measured the absorption and emission of EGFP. The regarding graph is given below (Figure 1).
 +
</p>
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<div class="center">
 +
<img src = "https://static.igem.org/mediawiki/2017/3/3f/T--Franconia--Parts--more2.png">
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<div>Figure 1: Fluorescence spectrum of EGFP showing absorption and emission at variant wavelengths.</div>
 +
</div>
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<p>The results show a difference in the wavelength of the absorption and the emission. The absorption of EGFP has its maximum at a wavelength of 487.5 nm and the emission maximum lays at a wavelength of 508.3 nm. The overlap of absorption and emission can be seen in the area around 500 nm. <br><br>
 +
We further plotted the measured values of the excitation wavelength and the emission wavelength of EGFP to obtain a height profile given in the diagram below (Figure 2).
  
<div class="column half_size">
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</p>
 
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<div class="center">
<h5>Inspiration</h5>
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<img src = "https://static.igem.org/mediawiki/2017/a/a3/T--Franconia--Parts--more1.png">
<p>We have a created  a <a href="http://parts.igem.org/Well_Documented_Parts">collection of well documented parts</a> that can help you get started.</p>
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<div>Figure 2: Excitation wavelength and emission wavelength of EGFP</div>
 
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</div>
<p> You can also take a look at how other teams have documented their parts in their wiki:</p>
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<p>The diagram displays the distribution of the different wavelengths. The red colored area reveals the overlap of excitation and emission at its uppermost distinctness.
<ul>
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</p>
<li><a href="https://2014.igem.org/Team:MIT/Parts"> 2014 MIT </a></li>
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<li><a href="https://2014.igem.org/Team:Heidelberg/Parts"> 2014 Heidelberg</a></li>
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<li><a href="https://2014.igem.org/Team:Tokyo_Tech/Parts">2014 Tokyo Tech</a></li>
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</ul>
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<h5>Part Table </h5>
 
 
<p>Please include a table of all the parts your team has made during your project on this page. Remember part characterization and measurement data must go on your team part pages on the Registry. </p>
 
 
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<groupparts>iGEM17 Franconia</groupparts>
 
  
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{{Franconia/Footer}}
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Latest revision as of 13:07, 1 November 2017

BBa_K2419000

SpyTag-ELP5-SnoopCatcher for elastomeric tissue

This part can be used to form an elastomeric tissue. The elastin like protein ELP5 as the main part has a SpyTag and a SnoopCatcher at its end to be able to bind its counterpart "SnoopTag-ELP5-SpyCatcher". Those two kind of proteins can build long polymer chains which can form an elastomeric tissue i.e. for the application as the basic tissue of artificial muscles.

BBa_K2419002

W51W54 for conductive pili production

This part can be used to express conductive pili of Geobacter Sulfurreducens in E.coli bacteria. Since the cultivation of Geobacter Sulfurreducens is difficult due to its strictly anaerobic demand, the expression of the pili in E.coli is the more convenient. The pili can then be used i.e. as the conductive layers of a dielectrical elastomeric actuator for the application of an artificial muscle.

BBa_K2419001

SpyTag-Streptavidin-ELP5-SnoopCatcher for elastomeric tissue connection with molecular machines

This part can be used to form an elastomeric tissue. The elastin like protein ELP5 as the main part has a SpyTag and a SnoopCatcher at its end to be able to bind its counterpart "SnoopTag-ELP5-SpyCatcher". Those two kind of proteins can build long polymer chains which can form an elastomeric tissue i.e. for the application as the basic tissue of artificial muscles. Additionally, the part contains a streptavidin tag for binding to i.e. biotin anchored molecular machines. This cross-linking enables the proteins to form an artificial muscle that can contract and relax in its structure by light stimuli through the mole cular machines.

BBa_K2419003

TagCFP for analysis of elastomeric tissue

TagCFP is a monomeric protein emitting bright cyan light. It is based on the natural fluorescence of the jellyfish Aequorea macrodactyla, which expresses a GFP-like fluorescent protein. This part can be used to analyze the quality i.e. of an elastomeric tissue out of proteins connected via Catcher-Tag systems (see BBa_K2419000). While such a tissue is formed, TagCFP as a fluorescent protein can be added due to its strong fluorescent emission. As a result, the maxima of emission and absorption of the fluorescent protein shift to a higher level when excited by the specific absorption light wavelength. This shift can only be ascribed to the assembly of TagCFP to the tissue. The behavior of the emission and absorption can therefore be used as a screen of the tissue around the fluorescent protein. The tissue network can be characterized regarding its structure and density. These parameters will give information about the quality of the polymeric network.

Testing the indicational function of TagCFP in an elastomeric tissue

To test the indicational function of TagCFP we created a hydrogel resembling the elastomeric tissue. We then added TagCFP both into water and the hydrogel. The results of this test are shown in Figure 1. On the right, TagCFP fluoresces in a cyan color when added to water and excited with light. Whereas the fluorescence color changes to a light blue when excited with light while being located in the hydrogel.

Figure 1: TagCFP in water (right) and TagCFP in hydrogel (left).

These results visibly show the effect of TagCFP being added to different solutions. The change of the color from cyan in water to light blue in the hydrogel indicates a shift of the emission maximum and therefore TagCFP can be used as a qualitatively test for elastomeric tissue, while additionally, further characterization of the tissue can be achieved. Characterization We further characterized the TagCFP to supply a broader understanding of the properties of this fluorescent protein. We therefore measured the absorption and emission of TagCFP. The regarding graph is given below (Figure 2).

Figure 2: Fluorescence spectrum of TagCFP showing absorption and emission at variant wavelengths.

The results show a difference in the wavelength of the absorption and the emission. The absorption of TagCFP has its maximum at a wavelength of 457.4 nm and the emission maximum lays at a wavelength of 478.1 nm. The overlap of absorption and emission can be seen in the area around 470 nm.
We further plotted the measured values of the excitation wavelength and the emission wavelength of TagCFP to obtain a height profile given in the diagram below (Figure 3).

Figure 3: Excitation wavelength and emission wavelength of TagCFP.

The diagram displays the distribution of the different wavelengths. The red colored area reveals the overlap of excitation and emission at its uppermost distinctness.

Further characterization of EGFP

We further characterized the “EGFP Protein Production Construct” (Part:BBa_K1123005) of the group iGEM13_TU-Eindhoven to supply a broader understanding of the properties of this fluorescent protein. We therefore measured the absorption and emission of EGFP. The regarding graph is given below (Figure 1).

Figure 1: Fluorescence spectrum of EGFP showing absorption and emission at variant wavelengths.

The results show a difference in the wavelength of the absorption and the emission. The absorption of EGFP has its maximum at a wavelength of 487.5 nm and the emission maximum lays at a wavelength of 508.3 nm. The overlap of absorption and emission can be seen in the area around 500 nm.

We further plotted the measured values of the excitation wavelength and the emission wavelength of EGFP to obtain a height profile given in the diagram below (Figure 2).

Figure 2: Excitation wavelength and emission wavelength of EGFP

The diagram displays the distribution of the different wavelengths. The red colored area reveals the overlap of excitation and emission at its uppermost distinctness.

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