Difference between revisions of "Part:BBa K3468041"
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3468041 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468041 SequenceAndFeatures</partinfo> | ||
− | + | Adding hydrogen bonds stabilized α4-β6loop | |
+ | The reduction of DDG was predicted by FoldX. PyOML was used for visual screening, which formed hydrogen bonds with 169-SER and 176-LEU. after mutation to ARG, he formed new hydrogen bonds with 172-ASN, which stabilized α4-β6loop and was beneficial to improve the thermal stability of PETase. | ||
+ | [[File:N173R.png|400px|thumb|left|Fig.1 N173R in PyMOL]] | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display |
Latest revision as of 13:28, 27 October 2020
PETase N173R
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 N to R at 173 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 α4-β6loop The reduction of DDG was predicted by FoldX. PyOML was used for visual screening, which formed hydrogen bonds with 169-SER and 176-LEU. after mutation to ARG, he formed new hydrogen bonds with 172-ASN, which stabilized α4-β6loop and was beneficial to improve the thermal stability of PETase.