Difference between revisions of "Part:BBa K3468088"

 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468088 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468088 SequenceAndFeatures</partinfo>
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Attempts to stabilize folded proteins have naturally focused on the use of disulfide bonds. These covalent crosslinks have a reputation for being able to stabilize folded conformations by between 2 and 5 kcal/mol for each disulfide. Disulfide bonds provide stability to many extracellular and secreted proteins. Disulfide bonds are believed to decrease the conformational entropy and raise the free energy of the denatured state, thus providing an increase in stability to the folded protein conformation. While the overall effect of a disulfide bond may be complex, including an enthalpic component, considerable evidence supports the long-standing hypothesis that stability is gained through a reduction in unfolded conformational entropy. In our design two parallel folds (β7-β8) of PETase were introduced to stabilize this region and improve the thermal stability of the protein
  
 
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Revision as of 06:32, 25 October 2020


PETase A202C&E231C

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 A202C/E231C 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]

Attempts to stabilize folded proteins have naturally focused on the use of disulfide bonds. These covalent crosslinks have a reputation for being able to stabilize folded conformations by between 2 and 5 kcal/mol for each disulfide. Disulfide bonds provide stability to many extracellular and secreted proteins. Disulfide bonds are believed to decrease the conformational entropy and raise the free energy of the denatured state, thus providing an increase in stability to the folded protein conformation. While the overall effect of a disulfide bond may be complex, including an enthalpic component, considerable evidence supports the long-standing hypothesis that stability is gained through a reduction in unfolded conformational entropy. In our design two parallel folds (β7-β8) of PETase were introduced to stabilize this region and improve the thermal stability of the protein