Difference between revisions of "Part:BBa K3610020:Design"
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===Design Notes=== | ===Design Notes=== | ||
Codons with a frequency lower than 10% were considered rare and were replaced for optimal expression. As alternative codons, the ones with the highest frequencies were chosen unless it added unwanted restriction sites and was therefore incompatible with iGEM standard. | Codons with a frequency lower than 10% were considered rare and were replaced for optimal expression. As alternative codons, the ones with the highest frequencies were chosen unless it added unwanted restriction sites and was therefore incompatible with iGEM standard. | ||
+ | |||
+ | Split was made at amino acids 158 and 159 of the full length mCherry. | ||
===Source=== | ===Source=== | ||
− | + | Provided by the Cyril Zipfel Lab, Switzerland | |
===References=== | ===References=== | ||
+ | Fan, Jin-Yu; Cui, Zong-Qiang; Wei, Hong-Ping; Zhang, Zhi-Ping; Zhou, Ya-Feng; Wang, Yun-Peng; Zhang, Xian-En (2008): Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein–protein interactions in living cells. In: Biochemical and Biophysical Research Communications 367 (1), S. 47–53. DOI: 10.1016/j.bbrc.2007.12.101. |
Latest revision as of 23:10, 27 October 2020
mCherry N-terminal - codon optimized for S. cerevisiae
- 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
Codons with a frequency lower than 10% were considered rare and were replaced for optimal expression. As alternative codons, the ones with the highest frequencies were chosen unless it added unwanted restriction sites and was therefore incompatible with iGEM standard.
Split was made at amino acids 158 and 159 of the full length mCherry.
Source
Provided by the Cyril Zipfel Lab, Switzerland
References
Fan, Jin-Yu; Cui, Zong-Qiang; Wei, Hong-Ping; Zhang, Zhi-Ping; Zhou, Ya-Feng; Wang, Yun-Peng; Zhang, Xian-En (2008): Split mCherry as a new red bimolecular fluorescence complementation system for visualizing protein–protein interactions in living cells. In: Biochemical and Biophysical Research Communications 367 (1), S. 47–53. DOI: 10.1016/j.bbrc.2007.12.101.