Part:BBa_K4430008:Design
GFP-TSP
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 1961
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 641
Design Notes
Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral TSP for attachment. GFP emits green fluorescence under the confocal laser scanning microscope. Using fusion protein GFP-TSP, we can confirm whether TSP binds strongly to the cell surfaces of SE. Commonly, when interdomain movement and association of fusion protein is desired, flexible linkers are a good choice. Flexible linkers are usually passive; they serve by retaining distance between functional protein motifs. The length of flexible linkers is the key property that determines the appropriate folding in fusion proteins, if not achieved, leads to the formation of non-functional aggregates. The combination of non-polar Gly residues with the polar Ser or Thr is routinely used for synthesizing the flexible linkers. The flexible linkers are proven helpful for stabilizing such types of neighbors by facilitating the covalent bonding among them. So the flexible linker GGSG was used as fusion protein linker in GFP-TSP.
Source
GFP is from BBa_K404316. Protein linker is from BBa_K4430004. TSP is from BBa_K4430003.