Part:BBa_K4380005
Introduction
Vilnius-Lithuania Igem 2022 project NanoFindused this part as a way to expose proteins onto the bacterial surface. 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 a peptide bound to a fluorescent protein, and another peptide is immobilized on a cellulose membrane by a cellulose binding domain. This linker was used to attach different proteins to their respective peptides.
Usage
This sequence is a linker can be used to accurately add certain domains with each other.
Biology
This linker which were expected to form a monomeric hydrophilic α-helix, were designed according to the previous study on a short peptide forming a monomeric α-helix (Marqusee and Baldwin, 1987) [1]. In that study, the best helix-forming peptide, AEAAAKEAAAKEAAAKA [(i+4)E,K], which was stabilized by Glu––Lys+ salt bridges, showed ~80% helicity.
17x Helix
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
References
[1]Marqusee, S., & Baldwin, R. L. (1987). Helix stabilization by Glu-...Lys+ salt bridges in short peptides of de novo design. Proceedings of the National Academy of Sciences, 84(24), 8898–8902. https://doi.org/10.1073/pnas.84.24.8898
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