Template:Team:Bonn:NetworkData

content.childs=[4,5,9,11,7,10];  

content.parents=[2]

content.parents=[2];

content.summary= "Direct binding of small molecules in order to activate or inactivate protein function";

content.text= "Direct binding of small molecules an activate or inactivate protein function";

content.text= "Moreover proteins can be regulated directly in many different ways. Binding of other Proteins or small molecules for example can activate or deactivate the catalytic function of proteins. For example small molecules can have great impact on protein function. They can often influence protein functions by binding to an allosteric center. Small molecules can be activating, as well as repressing, depending on the type of the molecule^{<a href=#11.1>11.1</a>}.</br></br><div class='content-image'> <img src='https://static.igem.org/mediawiki/2013/1/1c/BonnSmallMolecules.jpg' width='550'> </br>Different mechanisms for small-molecule activation of enzymes^{<a href=#11.2>11.2</a>} </div></br></br>The following picture shows the example of the allosteric activation of a glucokinase</br> <div class='content-image'> <img src=https://static.igem.org/mediawiki/2013/f/f4/BonnSmallMolecules2.jpg width='600'></br>&quot;(a) GK bound to the GKA, compound A, and glucose (blue, Protein Data Bank (PDB) ID 1V4S). Compound A binds at a site distal from the active site, which is highlighted by the presence of the substrate, glucose. (b) Structural overlay of GK in the presence of compound A and glucose with an unliganded, inactive GK (pink, PDB ID 1V4T). In the unbound GK, the GKA binding site is occluded. A large shift in the small subunit of GK occurs from the unbound to bound structures (black arrow). Glucose promotes the active conformation, which is hindered from shifting back to the inactive conformation in the presence of compound A. (c) 7 mutations (out of 13)9 identified in GK (pink) that are associated with disease map to the GKA binding site. These mutations highlight an important regulatory site within GK, and could similarly stabilize a closed, active conformation.&quot;^{<a href=#11.2>[11.2]</a>}</div></br></br><p><a name=11.1>11.1</a><a href='http://www.nature.com/nrd/journal/v3/n4/full/nrd1343.html'>Small-molecule inhibitors of protein–protein interactions: progressing towards the dream; Michelle R. Arkin & James A. Wells</a>/p></br><p><a name=11.2>11.2</a><a href='http://www.nature.com/nchembio/journal/v6/n3/full/nchembio.318.html'>Turning enzymes ON with small molecules, Julie A Zorn & James A Wells</a></p>";

content.text= "<b> Introduction: </b> </br>The ClpXP protein complex is an AAA+ protease, which means that it uses the energy of ATP hydrolysis to unfold and degrade marked proteins. The genetic code of this complex is highly conserved and can be found in human cells as well as in the bacteria Escherichia coli. The degradation system was discovered in the early 1990's and is now well established ^{<a href=#131>13.1</a>}.In our project we used ClpXP to degrade specific proteins in order to control their amount and effect. Therefor we utilized the common adaptor sspB. This protein recognizes substrates tagged with ssrA . In order to achieve a better control we made use of a sspB split system. For more detailed information about the ClpXP degradation system in our project go to ClpXP general. </br> </br> <b> Structure:  </b> </br> The ClpXP complex consists of two functional and structural different parts. The ClpX protein, an ATPase, is a hexameric ring (Fig.1) with a pore in the center<div align='lef'><img src='https://static.igem.org/mediawiki/2013/9/98/Bonn_Clp_Fig1.jpg' height='348' width='320'>Fig. 1: the hexameric ring of ClpX, each color represents a subunit, from  &quot;ClpXP, an ATP-powered unfolding and protein-degradation machine, Baker et al, Biochim Biophys Acta, 2012, PMCID: PMC3209554&quot;</div> </br> Each subunit contains a N-terminal domain (Fig.2, B), which assumes the adaptor recognition and is stabilized by coordinated zinc atoms.However, the important part of a subunit is the AAA+ module (Fig.2, C), divided in a large and a small domain. <div align='left'><img src='https://static.igem.org/mediawiki/2013/d/d0/BonnClp_Fig2.jpg' height='262' width='499'>Fig. 2: structure of a ClpX subunit, B: the N-terminal domain with brown zinc atoms, C: the AAA+ module, from  &quot;ClpXP, an ATP-powered unfolding and protein-degradation machine, Baker et al, Biochim Biophy Acta, 2012, PMCID: PMC3209554&quot;</div> </br> Between these domains the ATP binding site can be found, but not every subunit is able to bind the nucleotide. The arrangement of ATP binding and not-binding subunits in the hexameric ring is essential for the tertiary structure and the conformation changes after hydrolysis. The ClpP protein is a tetradecameric peptidase (Fig. 3, A and B).The subunits are arranged as two heptameric rings, one ring stacked on top of the other, with also a narrow pore in the center. This pore leads into the proteolytic chamber, which is barrel-shaped. Every subunit accommodates a classical Ser-His-Asp catalytic triad and oxyanion hole inside the chamber. Those proteolytic acitve sites (Fig. 3, C) can form several hydrogen bonds to the substrate ^{<a href=#131>13.1</a>}. <div align='left'><img src='https://static.igem.org/mediawiki/2013/0/06/BonnClp_Fig3.jpg' height='401' width='382'>Fig. 3: structure of ClpP, A: side view with stabilizing residues (blue), B: top view with the pore (red), C: active site of a subunit with a bonded substrate, from &quot;ClpXP, an ATP-powered unfolding and protein-degradation machine, Bakeret al, Biochim Bi phys Acta, 2012, PMCID: PMC3209554&quot;</div> </br> </br> </br><b> Functions: </b> </br>The ClpXP complex has three tasks to fulfill: </br> </br>1. Binding: The substrate binding process at the ClpX unit is normally conducted with the aid of an adaptor protein.This protein identifies tagged substrates and delivers them to the complex (Fig. 4, left). In order to transfer the protein, the adaptor also binds to the ClpX unit (Fig. 4, right), so that parts of the tag get approximated to a special binding site on the complex. After the linking between the tag and the binding site has been performed, the unfolding starts.The binding process also works without an adaptor protein, but an adaptor enhances the degratation by improving enzyme-substrate affinity. </br> </br> 2. Unfolding and translocation: The translocation of polypeptids through the ClpX unit to the ClpP chamber is an active process using energy from ATP-binding and -hydrolysing cycles. Therefor are several ATP molecules linked to the ClpXprotein. The separation of one phosphate molecule results in conformation changes, which pulls the linked protein more inside the pore located in the center of ClpX. The remaining ADP has to be replaced by a new ATP molecule before the cycle can start again. Meanwhile the unfolding is driven automatically, because the large tagged protein has to fit into the narrow pore, which forces the three-dimensional structure to become linear. </br> </br> 3. Degradation: The axial pore of the ClpP unit is also very narrow, allowing the entry of only small unfolded peptides into the proteolytic chamber. Inside the chamber, the substrate binds to an active site over several hydrogen bonds. It also can be linked to multiple active sites. In this position, proteins are cleaved in a maximum speed of around 10,000 proteins per minute by ClpP alone. If the ClpX unit is added, the rate is with ~0.2 proteins per minute and 0.3 &my;M substrate much lower, because the unfolding process takes more time ^{<a href=#131>13.1</a>} ^{<a href=132>13.2</a>}. </br> </br> <div align='left'><img src='https://static.igem.org/mediawiki/2013/b/b8/BonnClp_Fig4.jpg' height='311' width='628'>Fig. 4: Model of the degradation process with the sspB adaptor, from &quot;Engineering controllable protein degradation, McGinness et al, Molecular cell, 2006, PMID:16762842'</div> <h2><b> References </b> </h2></br> </br> <p><a name=131>13.1</a> ClpXP, an ATP-powered unfolding and protein-degradation machine, Baker et al, Biochim Biophys Acta, 2012, PMCID: PMC3209554</br> <a name=132>13.2</a> Flexible Linkers Leash the Substrate Binding Domain of SspB to a Peptide Module that Stabilizes DeliveryComplexes with the AAA ClpXP Protease, Wah et al, 2003, Molecular cell, PMID: 14536075</p></br>";  

content.text= "<b>Introduction </b> </br> The sspB protein is an adaptor responsible for delivering ssrA-tagged substrates to the ClpXP protease in order to enhance their degradation.Thus, bacterias like E.coli or C. crescentus regulate the concentration of marked proteins and also are in control of their quality. Even though degeneration of tagged substrates is possible without sspB, sspB delivering is a common process, because it improves the affinity between ssrA and ClpXP^{<a href='#14.1'>14.1</a>}. </br> In our project, we used a sspB split variant instead of the normal sspB in order to control cleaving rate. The two parts of this version only stay divided until we ray them with light of a special wavelength. After that, the fractions form an unit and can function normal from now on as described below. </br> </br><b>Structure </b> </br>The sspB adaptor is a homomeric dimer (Fig. 1), which means that itconsists of two identical domains. Together the domains form a pore with the ssrA binding sites inside. Each domain also owns a C-terminal tail ending in a ClpX binding module, called XP. The amino-acid sequence of XP is highly conserved so that mutations in it mostly cause extremely decrease in activity, whereas the linker sequence differs from species to species ^{<a href='#14.2'>14.2</a>}^{<a href='#14.3'>14.3</a>}. <div align='left'><img src='https://static.igem.org/mediawiki/2013/5/5c/BonnsspB_Fig2.jpg' height='202' width='403'>Fig. 1: Ribbon diagramm of the sspB dimer with a bound srrA-tagged protein, from 'Versatile modes of peptide recognition by the AAA+ adaptor protein SspB, Levchenko et al, 2005, nature structural and molecular biology, PMID: 15880122</div> </br> </br></br></br><b>Function</b></br> SspB enhances degradation of ssrA-tagged proteins by lowering the K_M. Thus, with a given substrate concentration sspB-mediated cleaving runs faster than without sspB (Fig. 2) </br> <div align='left'><img src='https://static.igem.org/mediawiki/2013/d/d8/BonnSspB_Fig1.jpg' height='232' width='371'>Fig. 2: Diagramm, shows the degradation rate of GFP-ssrA without sspB, with sspB and with two mutations, the given substrate concentration is 0.3 &my;M, from 'Flexible Linkers Leash the Substrate Binding Domain of SspB to a Peptide Module that Stabilizes Delivery Complexes with the AAA ClpXP Protease, Wah et al, Molecular Cell, 2003, PMID: 14536075' </div></br> Therefor, the sspB dimer contains a pore and while 'AADENY' is linked with the inside, the 'LAA'-domain (respectively 'DAS') faces outwards, free to bind ClpX (Fig. 3).</br> The affinity of this binding amounts around 20 &my;M, which suggests a relative strong  connection. The two extremely flexible ClpX binding tails with XP at the C-terminal end  dock on ClpX. So the 'LAA'- domain lies closely to ClpX's axial pore and can be bound to it. <div align='left'><img src='https://static.igem.org/mediawiki/2013/7/7c/BonnSsra_fig3.jpg' height='151' width='116'>Fig. 3: Model of sspB with a bound ssrA-tagged substrate, from 'Engineering controllable protein degradation, McGinness et al, Molecular cell, 2006, PMID:16762842' </div></br> To sum up, there are three bonds connecting the ssrA-sspB-ClpX-complex and making it relative stable: ssrA with sspB, sspB with ClpX and ssrA with ClpX. Hence follows a lower K_M than the direct binding process has^{<a href='#14.4'>14.4</a>}^{<a href='#14.5'>14.5</a>}. <h2> References </h2> <a id='14.1'>14.1</a>Bivalent Tethering of SspB to ClpXP Is Required for Efficient Substrate Delivery: A Protein-Design Study, Bolon et al, 2004, Molecular Cell, PMID: 14967151 </br><a id='14.2'>14.2</a>see above </br> <a id='14.3'>14.3</a> Flexible Linkers Leash the Substrate Binding Domain of SspB to a Peptide Module that Stabilizes Delivery Complexes with the AAA ClpXP Protease, Wah et al, Molecular Cell, 2003, PMID: 14536075 </br> <a id='14.4'>14.4</a> see above</br> <a id='14.6'>[14.5]</a> Altered Tethering of the SspB Adaptor to the ClpXP Protease Causes Changes in Substrate Delivery, McGinnes KE et al, The journal of Biological Chemistry, 2007, PMID: 17317664 </br> <a id='14.4'>14.4</a>  ClpXP, an ATP-powered unfolding and protein-degradation machine, Baker et al, Biochim Biophys Acta, 2012, PMCID: PMC3209554</br>";  

content.childs=[36,21,20];

content.parents=[18];

content.type="Background";

content.childs=[38,45,53,69,52,57,65,100,200];

content.summary= "We engineer a photoswitachble protein degradation system relying on the ClpXP protease system an a LOV domain from avena sativa";  

content.text= "A reliable, yet easily adaptable mechanism for controlling protein activity is key to most areas of life and medical science research. Still, the most common approaches suffer from various flaws. Knocking genes out using homologous recombination, knocking a gene down with RNA interference or modulating the behaviour of a protein with a chemical stimulus - just to name a few prominent methods - is either restricted to non-lethal genes, does not yield a big difference in activity, or is absolutely inaccurate and thus prone to secondary effects.</br></br> Would it not be great if one could turn off any protein, at any time, with little to no side effects? That is where iGEM Bonn 2013 and their project comes in. We aim to overcome the aforementioned difficulties by engineering a novel tool based on blue-light-inducible degradation of targeted proteins.</br></br>Our system relies on two key components: A tiny (just 15 amino acids!) tag that is fused to the C-Terminus of a protein of your choosing, and a light sensing LOV (Light, Oxygen and Voltage) domain from Avena sativa.</br></br> The advantages of our approach are obvious: Not only does the usage of light allow for a superior tempero-spatial control, but it is also much less prone to unwanted side effects than any chemical stimulus.</br> Furthermore, as we rely on a direct degradation of the targeted protein, we expect an onset of the desired effect which is much faster and at least as high as in common approaches.</br> Finally, as our system requires only a minor modification of your target protein we expect its function to not be impaired, and the tag to go unnoticed in functional observations.";  

content.type="Projekt";  

content.titleLong = "Ortholog ClpXP system in C. crescentus";

content.summary= "Using the ortholog ClpXP protein degradation system of C. crescentus in E. coli enables us to induce protein degradation in native E. coli without interfering with their natural system.";

content.titleShort = "^CcClpXP";

content.titleLong = "C. crescentus: ClpXP";

content.titleShort = "^CcsspB&alpha;";

content.titleLong = "C. crescentus: sspB&alpha;";

content.titleShort = "^CcsspB Split";  

content.titleLong = "sspB Split in C. crescentus";  

content.titleShort = "^CcSsrA";

content.childs=[];

content.titleLong = "Light inducible Kill-switch systems using toxin-antitoxin modules";

content.childs=[];

content.titleShort = "Plasmids";

content.titleLong = "A list of generated plasmids";

content.summary= "A list of each and every plasmid we designed combined with short summaries of their function";

content.titleLong = "The maz toxin-antitoxin system";

content.titleShort = "ccdAB";  

content.summary= "CcdB leads to double strand breaks in bacterial genomic DNA and thus is a potent toxin leading to cell death. ccdA compromises the toxic effect of ccdB.";  

content.text= "The family of the &quot;zinc finger&quot; proteins has a different approach of Transcription regulation. They contain a zinc ion as a cofactor. Zinc finger proteins have a DNA binding and a dimerization domain. They can be differentiated due to different loops. On the one hand they can bind to almost every part of DNA and on the other hand they can bind to several receptors. Hence the activating or repressing effect is not defined by the zinc finger itself, but by the effector Protein it is binding to^{<a href=#721>72.1</a>}. </br></br> <div class='content-image'> <img src='https://static.igem.org/mediawiki/2013/4/4b/BonnZincFinger.jpg' width='400' height='400'></br>&quot;The zinc ion (green) is coordinated by two histidine and two cysteine amino acid residues&quot;^{<a href=#722>72.2</a>}</div></br></br> <p><a name=721>72.1</a> <a href=http://www.pnas.org/content/early/2013/09/11/1303625110.long> Transcription factor ZBED6 affects gene expression, proliferation, and cell death in pancreatic beta cellsXuan Wang, Lin Jiang,Ola Wallerman, Ulla Engström, Adam Ameur, Rajesh Kumar, Gupt, YuQi, Leif Andersson and Nils Welsh Science for Life Laboratory, Department of Medical Cell Biology, and Science for Life Laboratory, Department of Medical Biochemistry and Microbiology, Uppsala University, SE-75123 Uppsala, Sweden; Ludwig Institute for Cancer Research Ltd., Science for Life Laboratory, Uppsala University, SE-751 24 Uppsala, Sweden; andScience for Life Laboratory, Department of Immunology, Genetics and Pathology, Uppsala University, SE-75185 Uppsala, Sweden </a> </p> </br> <p><a name=722>72.2</a> <a href='http://en.wikipedia.org/wiki/Zinc_finger'>Cartoon representation of the zinc-finger motif of proteins</a></p>";

content.text= "Tales are proteins which bind promoter sequences. Their DNA binding domain consists of several tandem repeats that are able to bind specific domains of the DNA. These tandem repeats can be engineered easily. Thus the user can define the domain to bind to. Very similar to the zinc finger they actually do not regulate transcription but bind effector proteins which are able to activate transcription. The great advance, in comparison to the zinc finger domain, is it's easy way of engineering. Scientists can regulate very specificlly transcription by the use of TALEs.</br></br><p> <a href='http://onlinelibrary.wiley.com/doi/10.1111/jipb.12091/abstract'> Site-Specific Gene Targeting Using Transcription Activator-Like Effector (TALE)-Based Nuclease in Brassica oleracea: Zijian Sun†,Nianzu Li†, Guodong Huang, Junqiang Xu, Yu Pan, Zhimin Wang, Qinglin Tang, Ming Song*, Xiaojia Wang> </a> </p>";

content.text= "SsrA and sspB are peptides that mediate proteolysis via the ClpXP protease system in bacteria. In this article and the related articles, the focus is on their orthologs in C. crescentus, being referred to as ^CcssrA and ^CcsspB&alpha;, respectively, omitting ^Cc when obvious out of context. The ClpXP protease has an important function in regulation of the cell division cycle by effective proteolysis of short-lived regulatory proteins.</br>A protein which needs to be degraded will be tagged with the amino acid peptide ^CcssrA which is added at its C-terminus during translation. ^{<a href=#741>74.1</a>, <a href=#742>74.2</a>} The ClpX subunit of the ClpXP protease recognizes the ssrA tag by specific binding and unfolds the tagged protein, in which ATP is hydrolyzed. In C. crescentus, the ssrA tag has a length of 14 amino acids, while the E. coli ortholog is only eleven amino acids long. </br>sspB&alpha; is a dimeric protein that serves as a tether which brings the ssrA tagged protein and the ClpXP protease together and therefore accelerates protein degradation. It simultaneously binds to both the ssrA tag and the ClpX subunit and in this way brings the tagged protein in close contact with the protease. </br></br><h2>References</h2></br><a name=741>74.1</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/11535833'>Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis, Flynn et al., Proceedings of the National Academy of Sciences of the United States of America, 2001, PMID: 11535833</a></br><a name=742>74.2</a> <a href='http://www.ncbi.nlm.nih.gov/pubmed/17937918'> Structure and substrate specificity of an SspB ortholog: design implications for AAA+ adaptors, Chien et al., Cell Press, 2007, PMID: 17937918</a>";

content.childs=[106,107,108,112,101,110,130];

content.summary= "For our Human Practice advances our project's design follows the well-known franchise of Star Wars - being inspired by the LOV domain our project name &quot;LOV WARS&quot; was born. The constant references to the Star Wars movies facilitate the access to synthetic biology to a person that is not familiar with the subject. We put great effort into adapting every aspect of our public presence to Star Wars.";  

content.titleShort = "Presentations"

content.titleShort = "Congress Berlin";

content.text = "<h1>Science Slam</h1><p>Our project aims to make versatile control of biological machines easily possible for everybody. During conception we wondered how our human practice work could represent that thought and decided to organize a science slam – an event which makes science available to everybody!</p><p>We believe that science must not only stay in laboratories and lecture halls but reach lots of people out there. And without a doubt, the walls of the reputed “ivory tower” couldn’t stand throughout the evening of our event!</p><p>Furthermore, the science slam provided a platform for our slammers to share the passion for their project with more than just their colleagues and thus help to popularize their field. In ten minutes, they presented their topic in a playful and inspirational manner and the audience decided which slammer has managed to get them carried away the most.</p><p>We managed not only to give floor to a large variety of fields by our slammers from physics, medicine, psychology, informatics, politics and engineering – but to make them be heard by a public which was very mixed indeed.</p><p>As a prelude to the event, we acquainted the audience with synthetic biology and our project by showing what synthetic biology can do for each of us. Distributed questionnaires during the evening showed that -as hoped- our presentation helped to leave a positive mark on the field of synthetic biology in people&apos;s heads:</p><p>For example, 97% of the people, who stated they did not know about synthetic biology before have got a proper picture of it during our event. 86% said, they are now familiar with the iGEM competition and everybody stated, they found the idea to combine the presentation of our iGEM project with a science slam “very good” or “good. </br> <p> <img src=https://static.igem.org/mediawiki/2013/d/df/Bonn_Science_Slam_1.png> </br> <p> <img src= https://static.igem.org/mediawiki/2013/f/f1/Bonn_Science_Slam_2.png> </br> <p> <img src=https://static.igem.org/mediawiki/2013/5/55/Bonn_Science_Slam_3.png></br> </p><p>The fact that our audience liked this topic had been reflected in our voting: Our representative for synthetic biology, Mogan Ramesh won the science slam. He originally comes from engineering but discovered his passion for “superbacteria e.coli” during his studies which he gladly shared with us. In ten minutes, he taught us that e.coli does not only work as “eeew” on our meal, but showed how his group studies on making e.coli work for us, e.g. producing pharmaceuticals.</p><p>How? For example, recombinant DNA technology can be used to modify Escherichia coli to produce human insulin. Mogans works within a group of scientist that investigate the metabolic network in the ‘Escherichia coli’ bacteria cell. Attempts to raise the copy number of plasmid DNA have been successful, and the goal now is to understand how the cell has accomplished this task. Proteomic studies have indicated an expected cellular adaptation that agrees with attempts to raise copy number in the literature; however, the thermodynamic implications of these results have been minimally explored. The “goal” of a cell remains controversial; one explanation is that the cellular metabolism seeks to maximize the entropy (minimize the Gibbs energy) of the system. Using GAMS as an optimization tool, it is explored if the reaction paths that have proven to be the most likely are also the paths that minimize the Gibbs energy of the system.</p><p>All in all, our science slam has been a great success which demanded a reenactment from a lot of sites.</p><p><b> Here are a few impressions from our event:</b></p><p> <img src=https://static.igem.org/mediawiki/2013/0/07/BonnScienceslam1.PNG> <br /><br /><i>Tobias Bald from experimental dermatology (University of Bonn) spoke about the “Dark side of the immune system”.</i></p><p><img src=https://static.igem.org/mediawiki/2013/d/dd/BonnScienceslam2.PNG><br /><br /><i>Prof. Dr. Herbert Dreiner gave us a review of “Fukushima” with full activity.</i></p><p><img src=https://static.igem.org/mediawiki/2013/0/0c/BonnScienceslam3.PNG><br /><br /><i>Our winner Mogan Ramesh shared his passion for “superbacteria e.coli”.</i></p><p><img src=https://static.igem.org/mediawiki/2013/2/24/BonnScienceslam4.PNG><br/><br/><i>Full house at our “Science Slam”.</i></p><p><img src=https://static.igem.org/mediawiki/2013/d/d5/BonnScienceslam5.PNG><br/><br/><i>Our audience obviously enjoyed the show.</i></p>";

content.parents=[100];

content.childs=[];

content.titleShort = "Schools";  

content.parents=[112];

content.childs=[];

content.titleShort = "Comic: About";

content.summary= "We introduced a hand drawn comic series called &quot;LOV Wars&quot; about Obi-Wan E. Coli and his adventures in the Galaxy of Petri. Basic concepts of synthetic biology are explained along the way.";

content.text="On the mission to find new and interesting means to bring across the concepts of synthetic biology, we introduced a comic series consisting of three episodes in the style of the well known Star Wars movies. The readers will find themselves in a world where Galaxies are petri dishes and all the characters are bacteria. Alongside the action-filled story we step by step introduce basic concepts of synthetic biology. The use of light sabers and laser guns also offered a great opportunity to embed our system of light-degradable proteins in the plot. At our presentations at schools and at our information booth it proved to be an ideal eye-catcher for passers-by and led to them wanting to know more about the subject. During the episodes the reader accompanies the hero Obi-Wan E. Coli and his Padawan Plasmida on their journey through the Galaxy of Petri. They are fighting the villain Darth Cherry and his companions, the clones. But we don&apos;t want to spoil the story for you, just read the comic yourself below."; content.type="Human Practice";

content.titleShort = "LOV-Wars Minigame</br>About";

content.parents = [100];

content.childs = [109];

content.text = "<img src=https://static.igem.org/mediawiki/2013/c/c1/Bonn_Comic_episode1_page1.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/a/ad/Bonn_Comic_episode1_page2.jpg  width=735px><img src=https://static.igem.org/mediawiki/2013/1/19/Bonn_Comic_episode1_page3.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/8/80/Bonn_Comic_episode1_page4.jpg  width=735px><img src=https://static.igem.org/mediawiki/2013/6/6c/Comic_EN_2.0_%281%29.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/8/84/Comic_EN_2.0_%282%29.jpg  width=735px><img src=https://static.igem.org/mediawiki/2013/9/97/Comic_EN_2.0_%283%29.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/1/19/Comic_EN_2.0_%284%29.jpg  width=735px><img src=https://static.igem.org/mediawiki/2013/8/8d/Bonn_Comic_EN_3.0_%281%29.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/5/58/Bonn_Comic_EN_3.0_%282%29.jpg  width=735px><img src=https://static.igem.org/mediawiki/2013/8/8c/Bonn_Comic_EN_3.0_%283%29.jpg width=735px><img src=https://static.igem.org/mediawiki/2013/b/b4/Bonn_Comic_EN_3.0_%284%29.jpg  width=735px>";

content.childs=[131,133,136,137,138];

content.titleLong = "Our city Bonn";  

content.summary= "Bonn is a beautiful city in North Rhine-Westphalia, Germany.";  

content.text= "Bonn has a long and eventful history. The city was founded by the Romans in the year 12 before Christ and continued to grow ever since. Bonn also was the birthplace of the famous musician and composer Beethoven and even was the Capitol of West Germany for 41 years. Today Bonn has around 300 000 habitants and has become the cultural of the region. It is set on the river Rhine very close to Cologne. Everybody gets smitten with its charm and unique mixture of tradition and modern lifestyle. The city&apos;s historic center and the setting close to the river Rhine turn it into a wonderful place to live and study.<p style='text-align:center;'>the city&apos;s slogan:</br><i>&quot;Stadt. City. Ville. Bonn&quot;</i></p></br><p><a href=https://static.igem.org/mediawiki/2013/0/0b/Bonn_by_night.JPG><div class='content-image'align='center'><img src='https://static.igem.org/mediawiki/2013/0/0b/Bonn_by_night.JPG' width='600'></a>Bonn by night ^{&copy;Jan Hansen}</div></p><p><div class='content-image'align='center'><a href=https://static.igem.org/mediawiki/2013/a/a6/Bonn_poppelsdorfer_schloss.JPG><img src='https://static.igem.org/mediawiki/2013/a/a6/Bonn_poppelsdorfer_schloss.JPG' width='600'></a>The university ^{&copy;Jan Hansen}</div><p><a href=https://static.igem.org/mediawiki/2013/0/0b/Bonn_by_night.JPG><div class='content-image'align='center'><img src='https://static.igem.org/mediawiki/2013/7/75/Bonn_beethoven.JPG' width='600'></a>The famous Beethoven statue in the city center ^{<a href=http://www.bone-diagenesis.org/moziloCMS/gallery.php?gal=Bonn-nbsp~Impressions>[source]</a>}</div></p><h2>References</h2><p><a name='1'>1.</a> <a href='http://www.bonn.de'>http://www.bonn.de</a></p><p><a name='2'>2.</a> <a href='http://de.wikipedia.org/wiki/Bonn'>http://de.wikipedia.org/wiki/Bonn</a></p>";  

content.parents = [100];

content.childs = [109];