Difference between revisions of "Part:BBa K3468045"
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<partinfo>BBa_K3468045 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468045 SequenceAndFeatures</partinfo> | ||
Adding hydrogen bonds stabilized α2-β3loop and α3-β5loop | Adding hydrogen bonds stabilized α2-β3loop and α3-β5loop | ||
| − | + | The reduction of DDG was predicted by FoldX. PyOML was used for visual screening, which formed hydrogen bond with 51-THR. after mutation to ARG, it formed hydrogen bond with 73-ASN and 148-LYS, which stabilized α2-β3loop and α3-β5loop, which was beneficial to improve the thermal stability of PETase. | |
| + | [[File:T72R.png|400px|thumb|left|Fig.1 T72R in PyMOL]] | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468045 parameters</partinfo> | <partinfo>BBa_K3468045 parameters</partinfo> | ||
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Latest revision as of 13:31, 27 October 2020
PETase T72R
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 R at 72 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]
Adding hydrogen bonds stabilized α2-β3loop and α3-β5loop The reduction of DDG was predicted by FoldX. PyOML was used for visual screening, which formed hydrogen bond with 51-THR. after mutation to ARG, it formed hydrogen bond with 73-ASN and 148-LYS, which stabilized α2-β3loop and α3-β5loop, which was beneficial to improve the thermal stability of PETase.
