Difference between revisions of "Team:DTU-Denmark/Tour Approach"
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<h1 class="bottomborder">Approach</h1> | <h1 class="bottomborder">Approach</h1> | ||
| + | <p>We wanted to create a proteolytic enzyme assay based on a linker sequence which contains a cleavage site for proteases, that are characteristic for the venom of different snakes.</p><br /> | ||
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| + | <p>Proteins that give off signals when a linker sequence is cleaved, are not a new invention. FRET (Föster resonance energy transfer) has been used for many years in research, to gain a better understanding of protein-protein interactions. | ||
| + | </p><br /> | ||
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| + | <p>The biosensor consists of a fusion protein. Inspired by the design of different FRET reporters, our fusion protein contains two larger protein domains, separated by a flexible linker containing one or more substrate sequences. However, unlike FRET reporters, where fluorescent proteins make up the two larger domains, the two large protein domains in our biosensor are a chromoprotein domain and a binding domain. The linker between the two domains is designed to contain the specific cleavage sites found through screening methods. | ||
| + | </p><br /> | ||
<a href="https://2017.igem.org/Team:DTU-Denmark/Tour_Introduction" class="tourPrev">Previous: Introduction</a> | <a href="https://2017.igem.org/Team:DTU-Denmark/Tour_Introduction" class="tourPrev">Previous: Introduction</a> | ||
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<li class="rightnavbarbtn"> | <li class="rightnavbarbtn"> | ||
| − | <a href="#approach"> | + | <a href="#approach"></a> |
</li> | </li> | ||
</ul> | </ul> | ||
Revision as of 18:03, 1 November 2017
Approach
We wanted to create a proteolytic enzyme assay based on a linker sequence which contains a cleavage site for proteases, that are characteristic for the venom of different snakes.
Proteins that give off signals when a linker sequence is cleaved, are not a new invention. FRET (Föster resonance energy transfer) has been used for many years in research, to gain a better understanding of protein-protein interactions.
The biosensor consists of a fusion protein. Inspired by the design of different FRET reporters, our fusion protein contains two larger protein domains, separated by a flexible linker containing one or more substrate sequences. However, unlike FRET reporters, where fluorescent proteins make up the two larger domains, the two large protein domains in our biosensor are a chromoprotein domain and a binding domain. The linker between the two domains is designed to contain the specific cleavage sites found through screening methods.
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