Difference between revisions of "Part:BBa K3468047"

 
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468047 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468047 SequenceAndFeatures</partinfo>
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This mutant undergoes proline substitution. Proline has a special ring structure, which can increase the rigidity of the loop, reduce the conformational entropy, and improve the thermal stability of the protein.
  
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Maestro website evaluated an result of -1.214,IMUTANT website evaluated a decrease result of -0.32, and an evaluation of FoldX also obtained a thermal stability improvement result of -0.47 kcal/mol.  And the result was not ideal.
  
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[[File:S233P.png|400px|thumb|left|Fig.1 S233P in PyMOL]]
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[[File:WT S233.png|400px|thumb|left|Fig.1 WT S233 in PyMOL]]
 
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K3468047 parameters</partinfo>
 
<partinfo>BBa_K3468047 parameters</partinfo>
 
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Latest revision as of 13:34, 27 October 2020


PETase S223P

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 P at 223 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 mutant undergoes proline substitution. Proline has a special ring structure, which can increase the rigidity of the loop, reduce the conformational entropy, and improve the thermal stability of the protein.

Maestro website evaluated an result of -1.214,IMUTANT website evaluated a decrease result of -0.32, and an evaluation of FoldX also obtained a thermal stability improvement result of -0.47 kcal/mol. And the result was not ideal.

Fig.1 S233P in PyMOL
Fig.1 WT S233 in PyMOL