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Team:Calgary/Sandbox/Notebook/Journal/Linker
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<p>This week we started to perform literature searches for our element of the project. Our goal is to find a way to link the TALE and ferritin elements of the project. We have decided that using a two part system is optimal as this would allow the ferritin subunits to self-assemble without having a TALE protein attached that could potentially interfere with this process. In order to accomplish this we have decided to use coiled-coils. The synthetic IAAL E3 and IAAL K3 coils (Litowski and Hodges, 2002) have been selected to accomplish this. These coils make use of hydrophobic regions composed of leucine and isoleucine to bind to each other (Figure 1). The specificity of these coils is conveyed by the presence of glutamic acid and lysine residue that limit the binding to the formation of coil heterodimers. | <p>This week we started to perform literature searches for our element of the project. Our goal is to find a way to link the TALE and ferritin elements of the project. We have decided that using a two part system is optimal as this would allow the ferritin subunits to self-assemble without having a TALE protein attached that could potentially interfere with this process. In order to accomplish this we have decided to use coiled-coils. The synthetic IAAL E3 and IAAL K3 coils (Litowski and Hodges, 2002) have been selected to accomplish this. These coils make use of hydrophobic regions composed of leucine and isoleucine to bind to each other (Figure 1). The specificity of these coils is conveyed by the presence of glutamic acid and lysine residue that limit the binding to the formation of coil heterodimers. | ||
| - | Based off of results from previous ferritin fusions (Kim et al., 2011) it was decided that a linker sequence was needed between the coils and their respective proteins to prevent any steric hindrance due to the size of the ferritin and TALE proteins. A flexible glycine rich linker lacking protease cut sites was selected from the registry (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K648013">BBa_K157013</a>) | + | Based off of results from previous ferritin fusions (Kim et al., 2011) it was decided that a linker sequence was needed between the coils and their respective proteins to prevent any steric hindrance due to the size of the ferritin and TALE proteins. A flexible glycine rich linker lacking protease cut sites was selected from the registry (<a href="http://parts.igem.org/wiki/index.php?title=Part:BBa_K648013" target="_blank">BBa_K157013</a>) |
</p> | </p> | ||
Revision as of 17:05, 30 August 2013
Linker Journal
Week 1: May 1 - May 3
This week we participated in a general molecular biology workshop to refresh our memory of techniques used in molecular biology.
Week 2: May 6 - May 10
We continued the molecular biology workshop. This week we also divided up into our respective groups for the project and decided research priorities.
Week 3: May 13 - May 17
This week we started to perform literature searches for our element of the project. Our goal is to find a way to link the TALE and ferritin elements of the project. We have decided that using a two part system is optimal as this would allow the ferritin subunits to self-assemble without having a TALE protein attached that could potentially interfere with this process. In order to accomplish this we have decided to use coiled-coils. The synthetic IAAL E3 and IAAL K3 coils (Litowski and Hodges, 2002) have been selected to accomplish this. These coils make use of hydrophobic regions composed of leucine and isoleucine to bind to each other (Figure 1). The specificity of these coils is conveyed by the presence of glutamic acid and lysine residue that limit the binding to the formation of coil heterodimers. Based off of results from previous ferritin fusions (Kim et al., 2011) it was decided that a linker sequence was needed between the coils and their respective proteins to prevent any steric hindrance due to the size of the ferritin and TALE proteins. A flexible glycine rich linker lacking protease cut sites was selected from the registry (BBa_K157013)
Week 4: May 20 - May 24
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Week 5: May 27 - May 31
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