Difference between revisions of "Part:BBa K3468076"
 
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This mutation increases the hydrogen bond near T116D. 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.
 
This mutation increases the hydrogen bond near T116D. 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 T116D 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:T116D.png|400px|thumb|left|Fig.1 T116D in PyMOL]]
 
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K3468076 parameters</partinfo>
 
<partinfo>BBa_K3468076 parameters</partinfo>
 
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Latest revision as of 14:02, 27 October 2020


PETase T116D

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 D at 116 position which can be more stable in higher temperature compared with the wild type.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

This mutation increases the hydrogen bond near T116D. 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 T116D and Jmol to find whether there is a new salt bridge. Finally we use Pymol to find out what interaction make it become stable.

Fig.1 T116D in PyMOL