Difference between revisions of "Part:BBa K305004:Design"
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===Design Notes===
 
===Design Notes===
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codon optimized for B. subtilis  
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The RBS sequence used in this part can be found in several ''B. subtilis'' genes and is known to efficiently initiate translation. The spacer sequence between the RBS and start codon originates form the ''B. subtilis'' wapA gene. The CDS was optimized for ''B. subtilis'' by the GenScript OptimumGeneTM software (see images).
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[[Image:H codon opt Groningen.jpg|200px|thumb|left|Frequency of optimal codons before optimization. The x-axis 100 value is set for the codon with the highest usage frequency for a given amino acid in ''B. subtilis''.]][[Image:H codon opt Groningen2.jpg|200px|thumb|left|Frequency of optimal codons after optimization. The x-axis 100 value is set for the codon with the highest usage frequency for a given amino acid in B. subtilis.]]
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===Structural Prediction===
 
===Structural Prediction===

Latest revision as of 18:21, 27 October 2010

Hydrophobic protein chaplin H (chpH)


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

The RBS sequence used in this part can be found in several B. subtilis genes and is known to efficiently initiate translation. The spacer sequence between the RBS and start codon originates form the B. subtilis wapA gene. The CDS was optimized for B. subtilis by the GenScript OptimumGeneTM software (see images).

Frequency of optimal codons before optimization. The x-axis 100 value is set for the codon with the highest usage frequency for a given amino acid in B. subtilis.
Frequency of optimal codons after optimization. The x-axis 100 value is set for the codon with the highest usage frequency for a given amino acid in B. subtilis.


Structural Prediction

Structural prediction of the protein without the signaling sequence by [http://zhanglab.ccmb.med.umich.edu/I-TASSER/ I-TASSER] yielded the following results. No tertiary structure has been identified by x-ray crystallography or NMR.

[http://zhanglab.ccmb.med.umich.edu/I-TASSER/output/S49455/ structural prediction] without signaling sequence

Source

Ordered as construct from Mr. Gene after genomic sequence had been identified.

References

Claessen, D; Rink, R; de Jong, W et al. 2003. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev 17 1714-1726