Difference between revisions of "Part:BBa K2719001:Design"
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<partinfo>BBa_K2719001 short</partinfo> | <partinfo>BBa_K2719001 short</partinfo> | ||
| + | <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" | ||
| + | <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> | ||
Revision as of 10:50, 17 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.
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Figure 2. Tenascin 5 domain V 3D structure, modelled with Swiss-Model
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
Optimized for E.coli BL21.
Source
Genomic Library