Difference between revisions of "Part:BBa K2382012"

(→‎Usage and Biology)
(→‎Usage and Biology)
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===Usage and Biology===
 
===Usage and Biology===
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The (EAAAK)5 linker is shown to possess a pH-dependent auto-cleavage feature. In the range pH 6–7, the
 
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target protein becomes automatically released from the fusion protein without proteolytic treatment.
 
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Although the mechanism of this auto-cleavage property of an (EAAAK)5 linker is unclear, this feature has
 
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been successfully employed for many cases of protein purification without the tag of a fusion protein.
 
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In our design, we use it as a rigid linker linking two proteins to form one fusion protein. It can prevent the
 
In our design, we use it as a rigid linker linking two proteins to form one fusion protein. It can prevent the
 
two proteins from interrupting each other while folding.
 
two proteins from interrupting each other while folding.
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A rigid linker that links two proteins to form one fusion protein. It repeats amino acids EAAAK
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three times to maintain distance of two proteins and preventing from interrupting each other
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while folding.
  
 
===Characterization of the EAAAK===
 
===Characterization of the EAAAK===

Revision as of 03:56, 30 October 2017

EAAAK



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
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 428
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

In our design, we use it as a rigid linker linking two proteins to form one fusion protein. It can prevent the two proteins from interrupting each other while folding. A rigid linker that links two proteins to form one fusion protein. It repeats amino acids EAAAK three times to maintain distance of two proteins and preventing from interrupting each other while folding.

Characterization of the EAAAK

References

Yue-Jin Wu, Chia-Ying Fan, Yaw-Kuen Li. Protein purification involving a unique auto-cleavage feature of a repeated EAAAK peptide. Journal of Chromatography B, 877 (2009) 4015–4021