Difference between revisions of "Part:BBa K3468068"
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===Usage and Biology=== | ===Usage and Biology=== | ||
| + | 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 46 at D position which can be more stable in higher temperature compared with the wild type. | ||
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This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability. | This mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability. | ||
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| + | We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable. | ||
| + | [[File:S46D.png|400px|thumb|left|Fig.1 S46D in PyMOL]] | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468068 parameters</partinfo> | <partinfo>BBa_K3468068 parameters</partinfo> | ||
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Latest revision as of 13:52, 27 October 2020
PETase S46D
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 mutation increases the hydrogen bond near S46. The hydrogen bond is an interaction formed by N, O and H in a protein, which can stabilize the structure of the protein and improve thermal stability.
We use FoldX to judge the thermal stability of S46D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.
