Difference between revisions of "Part:BBa K2719001:Design"
 
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__NOTOC__
 
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<partinfo>BBa_K2719001 short</partinfo>
 
<partinfo>BBa_K2719001 short</partinfo>
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<p>According to the information given from the phD Aurora Antonio, a beta-pleated sheet structure (antiparallel one) has a high level of stability but less than alpha-Helix. Also, it is possible to observe that this structure has many Random Coil, giving to the domain more flexibilite. In figure 1 you can see tenascin protein structure and it is conformed by beta-pleated antiparallel sheets and Random Coil, so that gives tenascin flexibility and stability. </p>
 
"https://static.igem.org/mediawiki/2018/3/30/T--TecCEM--TCD5DomainV3DStructure.png"
 
"https://static.igem.org/mediawiki/2018/3/30/T--TecCEM--TCD5DomainV3DStructure.png"
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<p><i>Figure 2.</i> Tenascin 5 domain V 3D structure, modelled with Swiss-Model</p>
  
 
<partinfo>BBa_K2719001 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2719001 SequenceAndFeatures</partinfo>
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===References===
 
===References===
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<p>Laporte L., Jeffrey J., et. al.(2013).<i>Tenascin C Promiscuously Binds Growth Factors via Its Fifth Fibronectin Type III-Like Domain</i>. March 14, 2018, of NCBI Website: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3630135/</p>
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<p>Gilpin, S. (2017) <i>Fibrillin-2 and Tenascin-C bridge the age gap in lung epitelial regeneration</i>. doi: 10.1016/j.biomaterials.2017.06.027.</p>
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<p>Midwood, K. et al. (2003) <i>Tissue repair and the dynamics of the extracelular matrix</i>. doi:10.1016/j.biocel.2003.12.003</p>
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<p>Midwood. K. et al. (2016) <i>Tenascin-C at a glance</i>. doi:10.1242/jcs.190546</p>
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<p>Gnanou, Y., Leibler, L., and Matyjaszewski, K. (2007). <i>Macromolecular Engineering. Precise Synthesis, Materials Properties, Applications</i>. Weinheim, Germany: WILEY-VCH Verlag GmbH & Co. KGaA</p>

Latest revision as of 03:21, 18 October 2018


Tenascin Domain V

According to the information given from the phD Aurora Antonio, a beta-pleated sheet structure (antiparallel one) has a high level of stability but less than alpha-Helix. Also, it is possible to observe that this structure has many Random Coil, giving to the domain more flexibilite. In figure 1 you can see tenascin protein structure and it is conformed by beta-pleated antiparallel sheets and Random Coil, so that gives tenascin flexibility and stability.

"T--TecCEM--TCD5DomainV3DStructure.png"

Figure 2. Tenascin 5 domain V 3D structure, modelled with Swiss-Model


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



Design Notes

Optimized for E.coli BL21.


Source

Genomic Library

References

Laporte L., Jeffrey J., et. al.(2013).Tenascin C Promiscuously Binds Growth Factors via Its Fifth Fibronectin Type III-Like Domain. March 14, 2018, of NCBI Website: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3630135/

Gilpin, S. (2017) Fibrillin-2 and Tenascin-C bridge the age gap in lung epitelial regeneration. doi: 10.1016/j.biomaterials.2017.06.027.

Midwood, K. et al. (2003) Tissue repair and the dynamics of the extracelular matrix. doi:10.1016/j.biocel.2003.12.003

Midwood. K. et al. (2016) Tenascin-C at a glance. doi:10.1242/jcs.190546

Gnanou, Y., Leibler, L., and Matyjaszewski, K. (2007). Macromolecular Engineering. Precise Synthesis, Materials Properties, Applications. Weinheim, Germany: WILEY-VCH Verlag GmbH & Co. KGaA