Difference between revisions of "Team:Tianjin"
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<p>Hydrophobins are proteins that are produced by filamentous fungi. They are characterized by having a hydrophobic patch on one part of the surface. Just because of this, a sea of possibilities are opened. Our project is mainly focused on its modification and new applications.</p> | <p>Hydrophobins are proteins that are produced by filamentous fungi. They are characterized by having a hydrophobic patch on one part of the surface. Just because of this, a sea of possibilities are opened. Our project is mainly focused on its modification and new applications.</p> | ||
| − | <li><p>1. Protein Modification</p> | + | <li><p>1.Protein Modification</p> |
<p>Natural hydrophobins couldn't be expressed by E.coli because of error of fold. However, it really restricts its broader application. To improve this condition, we re-designed the structures of two kinds of hydrophobins, making expression in E.coli possible.</p></li> | <p>Natural hydrophobins couldn't be expressed by E.coli because of error of fold. However, it really restricts its broader application. To improve this condition, we re-designed the structures of two kinds of hydrophobins, making expression in E.coli possible.</p></li> | ||
Revision as of 07:22, 23 July 2015
Project Description
Have you ever heard of the god of beginnings and transitions in ancient Roman myth? He is Janus, who is usually depicted as having two faces, since he looks to the future and to the past. Our project is focused on another Janus, a kind of protein, who looks to the hydrophilicity and to the hydrophobicity. Its scientific name is hydrophobin.
Hydrophobins are proteins that are produced by filamentous fungi. They are characterized by having a hydrophobic patch on one part of the surface. Just because of this, a sea of possibilities are opened. Our project is mainly focused on its modification and new applications.
1.Protein Modification
Natural hydrophobins couldn't be expressed by E.coli because of error of fold. However, it really restricts its broader application. To improve this condition, we re-designed the structures of two kinds of hydrophobins, making expression in E.coli possible.
2.Protein Chip
Another amazing characteristic of hydrophobins is that they are able to assemble spontaneously into amphipathic monolayers at hydrophobic-hydrophilic interfaces. Thus, we take this advantage to make a high-flux tumor detection chip. In this process, they could act as a medium in antibody-fixing by electrostatic force, which not only ensures the activity of antibody, but also improves the detections' accuracy rate.
3.Stimulate Plastic Degradation
Enzymatic hydrolysis of plastic has a broad developing prospect, however, the rate of hydrolysis is low due to many reasons. Some research has published that the cutinase degrading plastic could be enhanced by hydrophobins. In our experiment, we make them into a fusion to test if the effect could be better.
4.Protein Extraction
Because of hydrophobins' amphipathicity they could be used as a special purification tag for protein, and the purification system could be as simple as oil and water. With help of this, we could even achieve the recycle of enzymes used for plastic degradation.