Difference between revisions of "Part:BBa K3468044"
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | + | According to the prediction of FoldX, DDG decreased, and PyOML was used for visual screening, which formed hydrogen bonds with 132-ARG, 139-GLY and 140-THR. after mutating it into ASN, the number of hydrogen bonds increased, which stabilized α3-β5loop and was beneficial to improve the thermal stability of PETase. | |
+ | [[File:S136N.png|400px|thumb|left|Fig.1 S136N in PyMOL]] | ||
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3468044 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468044 SequenceAndFeatures</partinfo> | ||
− | + | Adding hydrogen bonds stabilized α3-β5loop | |
− | + | According to the prediction of FoldX, DDG decreased, and PyOML was used for visual screening, which formed hydrogen bonds with 132-ARG, 139-GLY and 140-THR. after mutating it into ASN, the number of hydrogen bonds increased, which stabilized α3-β5loop and was beneficial to improve the thermal stability of PETase. | |
+ | [[File:S136N.png|400px|thumb|left|Fig.1 S136N in PyMOL]] | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468044 parameters</partinfo> | <partinfo>BBa_K3468044 parameters</partinfo> | ||
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Latest revision as of 13:31, 27 October 2020
PETase S136N
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 N at 136 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-β5loop According to the prediction of FoldX, DDG decreased, and PyOML was used for visual screening, which formed hydrogen bonds with 132-ARG, 139-GLY and 140-THR. after mutating it into ASN, the number of hydrogen bonds increased, which stabilized α3-β5loop and was beneficial to improve the thermal stability of PETase.