Difference between revisions of "Part:BBa K3468016"
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After mutation, Q127L and M128, L131, V156 all have a new hydrophobic interaction, which can enhance the force between residues, enhance the hydrophobicity of the protein, and stabilize the protein structure. | After mutation, Q127L and M128, L131, V156 all have a new hydrophobic interaction, which can enhance the force between residues, enhance the hydrophobicity of the protein, and stabilize the protein structure. | ||
| − | [[File:Q127L111.png|400px|]] | + | [[File:Q127L111.png|400px|thumb|left|Fig.1 Q127 in PyMOL]] |
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| + | The result of thermal stability improvement was obtained by the evaluation of I-Mutant website, and the result of thermal stability improvement of -2.70057 was also obtained by FoldX evaluation. | ||
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| + | [[File:Q127L222.png|400px|thumb|left|Fig.2 Q127L in PyMOL]] | ||
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| + | [[File:Q127L2.png|400px|thumb|left|Fig.3 the result of Q127L in I-Mutant]] | ||
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<!-- Uncomment this to enable Functional Parameter display | <!-- Uncomment this to enable Functional Parameter display | ||
===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468016 parameters</partinfo> | <partinfo>BBa_K3468016 parameters</partinfo> | ||
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Latest revision as of 12:47, 27 October 2020
PETase Q127L
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 QtoL at 127 position which can be more stable in higher temperature compared with the wild type.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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. After mutation, Q127L and M128, L131, V156 all have a new hydrophobic interaction, which can enhance the force between residues, enhance the hydrophobicity of the protein, and stabilize the protein structure.
The result of thermal stability improvement was obtained by the evaluation of I-Mutant website, and the result of thermal stability improvement of -2.70057 was also obtained by FoldX evaluation.
