Difference between revisions of "Part:BBa K4380000:Design"
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The part comes from Clostridium thermocellum genomix sequence. | The part comes from Clostridium thermocellum genomix sequence. | ||
| − | [[Image: | + | [[Image:cbd.jpg|400px|thumb|right|Figure 1: First characterization experiment of the KlADH4-promoter (& eGFP) in ''S. cerevisiae''. After an overnight pre culture, the transformed yeast cells were transferred into SC-U Media with different ethanol concentration and the eGFP-fluorescence and the OD600 were measured at different times.]] |
===References=== | ===References=== | ||
Revision as of 22:26, 24 September 2022
Cellulose Binding domain (CBD)
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Design
Design Vilnius-Lithuania Igem 2022 team used this part as a novel way for peptide immobilization. The team was working to create an easily accessible nanoplastic detection tool, using peptides, whose interaction with nanoplastic particles would lead to an easily interpretable response. The system itself focused on smaller protein molecules, peptides, which are modified to acquire the ability to connect to the surface of synthetic polymers – plastics. The detection system works when peptides and nanoplastic particles combine and form a "sandwich" complex - one nanoplastic particle is surrounded by two peptides, attached to their respective protein. The sandwich complex consisted of two main parts – one is peptide bound to a fluorescent protein, other peptide immobilized on cellulose membrane by cellulose binding domain.
Source
Biology
The part comes from Clostridium thermocellum genomix sequence.
