Difference between revisions of "Part:BBa K3468068"
 
(3 intermediate revisions by the same user not shown)
Line 3: Line 3:
 
<partinfo>BBa_K3468068 short</partinfo>
 
<partinfo>BBa_K3468068 short</partinfo>
  
−
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 46 at D position which can be more stable in higher temperature compared with the wild type.
 
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===
 +
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 46 at D position which can be more stable in higher temperature compared with the wild type.
 +
  
 
<!-- -->
 
<!-- -->
Line 13: Line 14:
  
 
This mutation increases the hydrogen bond near S46. 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 S46. 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 S46D 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:S46D.png|400px|thumb|left|Fig.1 S46D in PyMOL]]
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  
 
===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K3468068 parameters</partinfo>
 
<partinfo>BBa_K3468068 parameters</partinfo>
 
<!-- -->
 
<!-- -->

Latest revision as of 13:52, 27 October 2020


PETase S46D


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 S46. 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 S46D 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 S46D in PyMOL