Difference between revisions of "Team:Linkoping Sweden"

 
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<a href="https://2018.igem.org/Team:Linkoping_Sweden">
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    <div class="menu-icon-container" ><h2 href"#">Main Menu&nbsp;&nbsp;&nbsp;&nbsp;<img src="https://static.igem.org/mediawiki/2018/c/c8/T--Linkoping_Sweden--menu-icon.png" alt="menu-icon"></h2> </div>
 
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       <ul class="liu-menu">
 
       <ul class="liu-menu">
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         <li><a  href="">Home</a></li>
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         <li><a  href="/Team:Linkoping_Sweden">Home</a></li>
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         <li class="dropdown"><a  href="/Team:Linkoping_Sweden/Project" class="dropbutton">Project</a>
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            <a  href="/Team:Linkoping_Sweden/Human_Practices" class="dropbutton">Human Practices</a>
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   <section class="home-home">
 
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      <h1 style="color:white" class="title">Welcome to our project
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       <span>This page is under construction</span>
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       The Folding Factory
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     <div class="home-project-textbox">
 
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       <h1>The Project</h1>
 
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       <p> The overexpression of recombinant proteins in E. coli often end up in inclusion bodies. Our project set out to investigate on how to prevent them. By using different chaperone systems, which are proteins that assist protein folding, protecting or disaggregating them during stress, a better yield of recombinant proteins can be achieved. Different combinations of these chaperone systems can have different results regarding the folding and aggregation of recombinant proteins. By testing combinations of these systems on hard-to-fold and aggregation prone proteins, a good understanding on how to prevent inclusion bodies can be obtained. </p>
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       <p> The expression of proteins in bacteria is a way to enable production of biofuels, large scale production in the pharmaceutical industry, and research. However, mass production of certain proteins in bacteria is hindered by protein size or the complex folding structure of proteins. <br><br> Protein folding has been shown to be assisted by chaperones, a protein aiding the expression of other proteins in bacteria. We illustrate this by co-expression of GroES and proteins that are problematic to express in E-coli. GroES is mostly known as a co-chaperone, but some studies indicate that it has a folding property on its own. We have aimed at investigating this further in order to create a system for expressing proteins in bacteria. We hope that our findings will give insight into sustainable ways for industrial protein production. </p>
 
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         <p>Model</p>
 
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         <p>Human Practice</p>
 
         <p>Human Practice</p>
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         <a href="/Team:Linkoping_Sweden/Human_practice" class="button button-accent button-small">Take me there!</a>
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<h1>Social Media</h1>
 
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Latest revision as of 16:11, 17 October 2018

LiU iGEM

The Folding Factory

The Project

The expression of proteins in bacteria is a way to enable production of biofuels, large scale production in the pharmaceutical industry, and research. However, mass production of certain proteins in bacteria is hindered by protein size or the complex folding structure of proteins.

Protein folding has been shown to be assisted by chaperones, a protein aiding the expression of other proteins in bacteria. We illustrate this by co-expression of GroES and proteins that are problematic to express in E-coli. GroES is mostly known as a co-chaperone, but some studies indicate that it has a folding property on its own. We have aimed at investigating this further in order to create a system for expressing proteins in bacteria. We hope that our findings will give insight into sustainable ways for industrial protein production.