Difference between revisions of "Part:BBa K3468034"
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===Usage and Biology=== | ===Usage and Biology=== | ||
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There is new hydrogen bond increased between T116R and T88, 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. | There is new hydrogen bond increased between T116R and T88, 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 T116R 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:T116R.png|400px|thumb|left|Fig.1 T116R in PyMOL]] | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468034 parameters</partinfo> | <partinfo>BBa_K3468034 parameters</partinfo> | ||
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Latest revision as of 13:09, 27 October 2020
PETase T116R
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 116 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]
There is new hydrogen bond increased between T116R and T88, 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 T116R and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.
