Difference between revisions of "Part:BBa K3468018"
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3468018 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3468018 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. | ||
| + | After mutation, N275I and P276, F284 all have new hydrophobic interactions, which can enhance the force between residues, enhance the hydrophobicity of the protein, and stabilize the protein structure. | ||
| − | + | The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -0.691164 was also obtained by the FoldX evaluation. | |
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K3468018 parameters</partinfo> | <partinfo>BBa_K3468018 parameters</partinfo> | ||
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Latest revision as of 12:59, 27 October 2020
PETase N275I
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 N to I at 275 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, N275I and P276, F284 all have new hydrophobic interactions, which can enhance the force between residues, enhance the hydrophobicity of the protein, and stabilize the protein structure.
The thermal stability improvement result was obtained by the evaluation of I-Mutant website, and the thermal stability improvement result of -0.691164 was also obtained by the FoldX evaluation.