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. | ||
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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:
- 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. Pro is in α helix N1 for better helix formation, but Ser121 is in α helix N2.