Difference between revisions of "Part:BBa K3468080"
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<partinfo>BBa_K3468080 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468080 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. The pro is better in the alpha helix N1, but Ser92 is in the alpha helix N2. | ||
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Latest revision as of 14:06, 27 October 2020
PETase S92P
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 92 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. The pro is better in the alpha helix N1, but Ser92 is in the alpha helix N2.