Difference between revisions of "Part:BBa K3468030"
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3468030 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468030 SequenceAndFeatures</partinfo> | ||
| + | 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. It has a side aromatic effect with F229, which can enhance the force between residues and stabilize the protein. | ||
| + | The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -0.3866 was also obtained by the FoldX evaluation. | ||
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Latest revision as of 13:03, 27 October 2020
PETase Y219W
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 Y to W at 219 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. It has a side aromatic effect with F229, which can enhance the force between residues and stabilize the protein.
The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -0.3866 was also obtained by the FoldX evaluation.