Difference between revisions of "Part:BBa K3468035"

 
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K3468035 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3468035 SequenceAndFeatures</partinfo>
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Usage and Biology
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Hydrophobic interaction is the main driver of protein folding. The phenomenon of hydrophobic groups gathering close to each other to avoid water is called hydrophobic interaction. The protein is stable in water when the hydrophobic side chains of the protein aggregate inside the protein, rather than being solvated by water. Hydrophobic interactions play a major role in maintaining protein conformation because water molecules interact more strongly with each other than with other nonpolar molecules. Nonpolar side chains gather inside protein molecules to avoid water. At the same time, most polar side chains maintain contact with water on the surface of the protein. The hydrophobic properties within the molecule not only explain the accumulation of hydrophobic residues, but also explain the stability of the spiral and fold plates.
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Maestro website evaluated an improvement result of 0.325, and an evaluation of FoldX also obtained a thermal stability improvement result of -1.156 kcal/mol. And the result was ideal.
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[[File:T198.png|400px|thumb|left|Fig.1 T198 in PyMOL]]
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[[File:T198V.png|400px|thumb|left|Fig.1 T198V in PyMOL]]
  
  

Latest revision as of 13:10, 27 October 2020


PETase T198V

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 V at 198 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]

Usage and Biology Hydrophobic interaction is the main driver of protein folding. The phenomenon of hydrophobic groups gathering close to each other to avoid water is called hydrophobic interaction. The protein is stable in water when the hydrophobic side chains of the protein aggregate inside the protein, rather than being solvated by water. Hydrophobic interactions play a major role in maintaining protein conformation because water molecules interact more strongly with each other than with other nonpolar molecules. Nonpolar side chains gather inside protein molecules to avoid water. At the same time, most polar side chains maintain contact with water on the surface of the protein. The hydrophobic properties within the molecule not only explain the accumulation of hydrophobic residues, but also explain the stability of the spiral and fold plates.

Maestro website evaluated an improvement result of 0.325, and an evaluation of FoldX also obtained a thermal stability improvement result of -1.156 kcal/mol. And the result was ideal.

Fig.1 T198 in PyMOL
Fig.1 T198V in PyMOL