Difference between revisions of "Part:BBa K3468084"
 
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===Usage and Biology===
 
===Usage and Biology===
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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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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468084 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468084 SequenceAndFeatures</partinfo>
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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 A40P, it was found that the thermal stability of the enzyme increased.
  
 
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Latest revision as of 14:09, 27 October 2020


PETase A40P

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 A to P at 40 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 A40P, it was found that the thermal stability of the enzyme increased.