Difference between revisions of "Part:BBa K3468085"
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<partinfo>BBa_K3468085 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468085 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. | |
+ | Using FoldX and I-Mutant to predict the stability of S142P, it was found that the stability decreased, and the result was not ideal. | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468085 parameters</partinfo> | <partinfo>BBa_K3468085 parameters</partinfo> | ||
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Latest revision as of 14:09, 27 October 2020
PETase S142P
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 142 position which can be more stable in higher temperature compared with the wild type.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE 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.