Difference between revisions of "Part:BBa K3468079"
| (One intermediate revision by one other user not shown) | |||
| Line 11: | Line 11: | ||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3468079 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468079 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 T113P, it was found that the thermal stability did not improve. The reason is that Thr113 is located at the i position of βturn. | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
Latest revision as of 14:04, 27 October 2020
PETase T113P
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 T to P at 113 position which can be more stable in higher temperature compared with the wild type.
Sequence and Features
Assembly Compatibility:
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 240
- 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 240
- 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 240
- 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 240
- 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 240
- 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 T113P, it was found that the thermal stability did not improve. The reason is that Thr113 is located at the i position of βturn.