Difference between revisions of "Team:KAIT Japan/Project"

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<div id="page body">
 
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<h1>タイトル</h1>
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<h3><a href="https://2015.igem.org/Team:KAIT_Japan"><img src="https://static.igem.org/mediawiki/2015/thumb/5/54/%E3%83%AD%E3%82%B4%E3%83%9E%E3%83%BC%E3%82%AF.jpg/800px-%E3%83%AD%E3%82%B4%E3%83%9E%E3%83%BC%E3%82%AF.jpg"  width="90px" height="70px"></a><FONT size="11">Project</FONT></h3>
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    <p>私はＨＰを作成している。</p><br>
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&nbsp;　In this year, we use the fluorescent protein, “Dronpa“, to make protein regulation system. <br>
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&nbsp;　Dronpa has photochromism, Dronpa able to change its state bright from dark or dark from bright.  Dronpa normally absorbs at 503 nm and emits green fluorescence, strong irradiation at 488 nm can convert this protein to a nonfluorescent state that absorbs at 390 nm. The protein can then be switched back to the original emissive state with minimal irradiation at 405 nm.<br>
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&nbsp;　We use Dronpa145N which is Lys145Asn mutant of Dronpa. At the bright state, this protein forms tetramer. While at dark state, Dronpa145N form monomer. The ensemble absorption and mission properties of Dronpa145N are highly similar to those of Dronpa. We utilize this conformation change for Light-dependent regulation of flexibility in a protein.<br>
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&nbsp;　Lys145Asn mutation effect the oligomerization-interface of this protein. In Dronpa, a high degrees of freedom of Lys145 make repulsion between one protomer and another protomer. But in Dronpa145N, it’s repulsion is fewer than Dronpa, because Asn145 has fewer degrees of freedom compared with Lys145’s it. Therefor Dronpa145N is able to tetramerization.<br>
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&nbsp;　We make a protein which is put some protein between Dronpa145N. When the Dronpa145N is dark state, the put protein’s conformation is steady. While when the Dronpa145N is bright state, it’s conformation is wry, because connection of both ends Dronpa145N bend the put protein. As a result, the put protein’s flexibility is reduced.
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      <p style="color:#0000FF">私はＨＰを作成している。</p><br>
 
  
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<br>
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<font size="5">Link list</font>
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<br>
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<ul>
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<li><a href="https://2015.igem.org/Team:KAIT_JAPAN">Atribution</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Team">Team</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Results">Results</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Parts">Parts</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Description">Protocol</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Notebook">Lab note</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Safety">Safety</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Human Practice">Human Practice</a></li>
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<li><a href="https://2015.igem.org/Team:KAIT_Japan/Judge">Judge</a></li>
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</ul>
  
  
  
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</div>
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<div class="asaide" id="side2">
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<br>
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<br>
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<font size="5">Sponsor</font>
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<br>
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<a href="http://www.cosmobio.co.jp/index_e.asp"><img src="https://static.igem.org/mediawiki/2015/6/62/Cosumo_bio.png" width="180px"></a>
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<br>
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<a href="http://www.kait.jp/yumepro/"><img src="https://static.igem.org/mediawiki/2015/0/07/Yumepuro.png" width="180px"></a>
  
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Latest revision as of 07:46, 8 September 2015

Project



 　In this year, we use the fluorescent protein, “Dronpa“, to make protein regulation system.
 　Dronpa has photochromism, Dronpa able to change its state bright from dark or dark from bright. Dronpa normally absorbs at 503 nm and emits green fluorescence, strong irradiation at 488 nm can convert this protein to a nonfluorescent state that absorbs at 390 nm. The protein can then be switched back to the original emissive state with minimal irradiation at 405 nm.
 　We use Dronpa145N which is Lys145Asn mutant of Dronpa. At the bright state, this protein forms tetramer. While at dark state, Dronpa145N form monomer. The ensemble absorption and mission properties of Dronpa145N are highly similar to those of Dronpa. We utilize this conformation change for Light-dependent regulation of flexibility in a protein.
 　Lys145Asn mutation effect the oligomerization-interface of this protein. In Dronpa, a high degrees of freedom of Lys145 make repulsion between one protomer and another protomer. But in Dronpa145N, it’s repulsion is fewer than Dronpa, because Asn145 has fewer degrees of freedom compared with Lys145’s it. Therefor Dronpa145N is able to tetramerization.
 　We make a protein which is put some protein between Dronpa145N. When the Dronpa145N is dark state, the put protein’s conformation is steady. While when the Dronpa145N is bright state, it’s conformation is wry, because connection of both ends Dronpa145N bend the put protein. As a result, the put protein’s flexibility is reduced.



















Sponsor