Coding

Part:BBa_K4439013

Designed by: Pauline Verchinine   Group: iGEM22_EPFL   (2022-09-29)
Revision as of 01:49, 12 October 2022 by Charlottedml (Talk | contribs)

mSA-GFP-CBD-10xHis


Abstract

To complete

Sequence and features


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]

Protein Characterization

Usage and Biology

Modeling


Model 03a.jpeg
Figure 9 : AlphaFold2 prediction for 03a. (A) First rank 3D model prediction of 03a protein; the iteration who got the highest score in the modeling. (B) Different correlation graphs between the query sequence of 03a and the predicted one, for each proposed 5 models. (C) Figure of sequence coverage of 03a and indices on alignment with other sequences in the mSA. (D) IDDT graph for 03a per residue to get an idea of the confidence in the model in predicting.

  • Analysis

In (fig.9, A), we could identify the three main parts of the mSA-GFP-CBD protein. Compared to the previous (fig.9, A) we could see that the GFP domain, in green, is more easily characterized and would yield a closer linkage to the mSA chain, in blue. So we will have both of the proteins closely associated. However for the CBD region, we identified a longer linkage which would mean different configuration of tha attachment possible. From (fig.9, B, D) it was really interesting to see that the 5 predictions yielded similar correlation measures and similar IDDT scores, which enabled us to confirm that the model is robust in the determination of three chain structures. The linkage would give in reality more freedom of placement of those chains.

Results

Bacterial Transformation

Protein Purification

Cloning by PCR and KLD

References

[edit]
Categories
Parameters
None