Difference between revisions of "Part:BBa K3468089"

 
 
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===Usage and Biology===
 
===Usage and Biology===
 
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Disulfide bonds are introduced near the N-terminal to stabilize the n-terminal alpha helix.
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468089 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468089 SequenceAndFeatures</partinfo>
 
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Disulfide bonds are introduced near the N-terminal to stabilize the n-terminal alpha helix.
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During Pymol visual examination, it was found that the mutation site was far away from the inside of the protein, which met the disulfide bond geometric standard, but destroyed the existing salt bridge (E44-K252). DDG is 0.663kcal/mol evaluated by FoldX.
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[[File:Fig5.png|400px|thumb|left|Fig.5 Structure feature of L43C and K252C]]
  
 
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Latest revision as of 14:16, 27 October 2020


PETase L43C&K252C

The PETase is an enzyme, which can hydrolyze PET and this mutation protein is changed on the basis of the PETase. This protein is changed L43C&K252C which can be more stable in higher temperature compared with the wild type.


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
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]
Disulfide bonds are introduced near the N-terminal to stabilize the n-terminal alpha helix.

During Pymol visual examination, it was found that the mutation site was far away from the inside of the protein, which met the disulfide bond geometric standard, but destroyed the existing salt bridge (E44-K252). DDG is 0.663kcal/mol evaluated by FoldX.

Fig.5 Structure feature of L43C and K252C