Part:BBa_K5310005:Design
(Gly4Ser)3 flexible linker
- 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 Notes
There have been recorded instances in literature where this linker failed to limit the interaction between neighbouring domains or limited protein expression (see Maeda, Y. et al, 1997 with a G-Vargula luciferase fusion protein [4] and Amet, N.et al, 2009 with a Tf-granulocyte colony stimulating factor (G-CSF) fusion protein [3]). The functional mishap in these examples was attributed to the need of a more rigid linker to keep a better distance between domains.
Source
Argos, P. 1990 and Chen, X. et al, 2013 have suggested synthetic Glycine-Serine fusion linkers for their stability and flexibility.
References
1. Chen, X., Zaro, J. L., & Shen, W. (2013). Fusion protein linkers: Property, design and functionality. Advanced Drug Delivery Reviews, 65(10), 1357-1369. https://doi.org/10.1016/j.addr.2012.09.039
2. Argos, P. (1990). An investigation of oligopeptides linking domains in protein tertiary structures and possible candidates for general gene fusion. Journal of Molecular Biology, 211(4), 943-958. https://doi.org/10.1016/0022-2836(90)90085-Z
3. Amet, N., Lee, HF. & Shen, WC. Insertion of the Designed Helical Linker Led to Increased Expression of Tf-Based Fusion Proteins. Pharm Res 26, 523–528 (2009). https://doi.org/10.1007/s11095-008-9767-0
4. Maeda, Y., Ueda, H., Kazami, J., Kawano, G., Suzuki, E., & Nagamune, T. (1997). Engineering of Functional Chimeric Protein G–VargulaLuciferase. Analytical Biochemistry, 249(2), 147-152. https://doi.org/10.1006/abio.1997.2181