Difference between revisions of "Part:BBa K3468083"

 
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<partinfo>BBa_K3468083 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468083 SequenceAndFeatures</partinfo>
 
This mutant undergoes proline substitution. Proline has a special ring structure, which can increase the rigidity of the loop, reduce the conformational entropy, and improve the thermal stability of the protein.
 
This mutant undergoes proline substitution. Proline has a special ring structure, which can increase the rigidity of the loop, reduce the conformational entropy, and improve the thermal stability of the protein.
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Using FoldX and I-Mutant to predict the stability of S142P, it was found that the stability decreased, and the result was not ideal. Pro is in α helix N1 for better helix formation, but Ser121 is in α helix N2.
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  

Latest revision as of 14:08, 27 October 2020


PETase S121P

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 from S to P at 121 position 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]

This mutant undergoes proline substitution. Proline has a special ring structure, which can increase the rigidity of the loop, reduce the conformational entropy, and improve the thermal stability of the protein.

Using FoldX and I-Mutant to predict the stability of S142P, it was found that the stability decreased, and the result was not ideal. Pro is in α helix N1 for better helix formation, but Ser121 is in α helix N2.