Difference between revisions of "Part:BBa K2719001:Design"
(→‎References)
Line 21: Line 21:
  
 
===References===
 
===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/

Revision as of 02:42, 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/