Types | DnaRegion
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Roles | Project
engineered_region
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Sequences | BBa_K2140004_sequence (Version 1)
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Description
This part contains the gene sequence for an alternative Double Helix StarScaffold design in which the original helix where the dimerization domain is based has been altered by lengthening the coil and changing the positions of the Asn residue used to promote antiparallel structure. The single coiled coil ???prototype??? version might be preferable because of the complication to structure and disulphide bond formation caused by four helixes total in each protein. However, the dHelix part has the advantage of avoiding the increased coiled coil stability due to the lengthening of the helix in the Prototype part. It also may have superior in vivo disulphide formation thanks to the extra secondary structure around the cysteines acting to potentially exclude disulphide bond isomerases.
Notes
The length of the linker and leucine zipper regions along with the order of the intein segments.
Source
The Leucine Zipper, Linker and Cystine regions we're designed denovo from the literature, while The inteins are a combination of engineered and non-engineered genomic gene segments.
1. Stevens, A. J., Brown, Z. Z., Shah, N. H., Sekar, G., Cowburn, D., & Muir, T. W. (2016). Design of a Split Intein with Exceptional Protein Splicing Activity. Journal of the American Chemical Society, 138(7), 2162-2165.
2. Carvajal-Vallejos, P., Palliss??, R., Mootz, H. D., & Schmidt, S. R. (2012). Unprecedented rates and efficiencies revealed for new natural split inteins from metagenomic sources. Journal of Biological Chemistry, 287(34), 28686-28696.
3. Dassa, B., London, N., Stoddard, B. L., Schueler-Furman, O., & Pietrokovski, S. (2009). Fractured genes: a novel genomic arrangement involving new split inteins and a new homing endonuclease family. Nucleic acids research, gkp095.