Difference between revisions of "Part:BBa K3468069"
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<partinfo>BBa_K3468069 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468069 SequenceAndFeatures</partinfo> | ||
Adding hydrogen bonds stabilized α3 helix and β3-α2loop | Adding hydrogen bonds stabilized α3 helix and β3-α2loop | ||
| + | According to the prediction by FoldX, DDG decreased, and PyOML was used for visual screening, which did not form hydrogen bonds. after it was mutated into ASP, it formed hydrogen bonds with 92-SER and 93-SER, which stabilized α3 helix and β3-α2loop, which was beneficial to improve the thermal stability of PETase. | ||
| + | [[File:R90D.png|400px|thumb|left|Fig.1 R90D in PyMOL]] | ||
<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
Latest revision as of 13:53, 27 October 2020
PETase R90D
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 R to D at 90 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 α3 helix and β3-α2loop According to the prediction by FoldX, DDG decreased, and PyOML was used for visual screening, which did not form hydrogen bonds. after it was mutated into ASP, it formed hydrogen bonds with 92-SER and 93-SER, which stabilized α3 helix and β3-α2loop, which was beneficial to improve the thermal stability of PETase.
