Difference between revisions of "Part:BBa K2384003"
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Our sequence optimization is based on the sequence provided by Peking University's IGEM VIKI in 2010.It is more suitable for expression in Bacillus | Our sequence optimization is based on the sequence provided by Peking University's IGEM VIKI in 2010.It is more suitable for expression in Bacillus | ||
+ | |||
+ | <b>Optimization Report</b> | ||
+ | |||
+ | 1.Codon Used Adjustment | ||
+ | The best value is 1 for sequence optimization. | ||
+ | |||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)1.png|thumb|400px|'''Before Codon Adjustment''']]</th> | ||
+ | </tr></table> | ||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)2.png|thumb|400px|'''After Codon Adjustment''']]</th> | ||
+ | </tr></table> | ||
+ | |||
+ | |||
+ | 2.Codon Used Distribution | ||
+ | Show the relative codon used distribution | ||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)3.png|thumb|400px|'''Before Optimization''']]</th> | ||
+ | </tr></table> | ||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)4.png|thumb|400px|'''After Optimization''']]</th> | ||
+ | </tr></table> | ||
+ | |||
+ | 3.GC Content: | ||
+ | The comparison of GC content between original sequence and optimized sequence | ||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)5.png|thumb|400px|'''Before Optimization''']]</th> | ||
+ | </tr></table> | ||
+ | |||
+ | <table><tr> | ||
+ | <th>[[Image:T--FAFU-CHINA--DSBA-MBP(Pb)(Pb)6.png|thumb|400px|'''After Optimization''']]</th> | ||
+ | </tr></table> | ||
+ | |||
<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== |
Revision as of 14:38, 1 November 2017
DsbA+MBP(Pb)
the periplasm display protein Dsba-MBP, which binding the lead of the enviroment. Disulfide bond formation protein A (DsbA) is a powerful oxidative protein of the thioredoxin family. DsbA can help protein to fold correctly both in vivo and in vitro 。The C-terminal fusion protein of the maltose-binding protein can be efficiently and rapidly output into the periplasm as a key component of the expression of the metal-binding peptide of the cyclin.
Our sequence optimization is based on the sequence provided by Peking University's IGEM VIKI in 2010.It is more suitable for expression in Bacillus
Optimization Report
1.Codon Used Adjustment The best value is 1 for sequence optimization.
2.Codon Used Distribution
Show the relative codon used distribution
3.GC Content: The comparison of GC content between original sequence and optimized sequence
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 255
Illegal BglII site found at 267 - 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]