Difference between revisions of "Part:BBa K3468087"
 
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<partinfo>BBa_K3468087 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468087 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 S141P, it is found that the thermal stability has been improved to a certain extent.
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  

Latest revision as of 14:14, 27 October 2020


PETase S141P

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 141 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 S141P, it is found that the thermal stability has been improved to a certain extent.