Part:BBa_K5357004
(GGGGS)3 Linker
Usage and Biology
Many important considerations must be accounted for when designing fusion proteins. One of these is in deciding what linker is best to attach the two proteins. There are broadly two options: a rigid linker, or a flexible linker. An example of a flexible linker is one made of glycine (G) and serine (S) residues. These linkers can be made of a variable number and ratio of these amino acids to tailor the exact characteristics of the linker. More glycine residues increase the flexibility of the linker. The combination of having both hydrophobic (G) and hydrophilic (S) residues prevents the formation of any secondary structure, and this reduces the risk of the linker interfering with the correct folding of the proteins it is connecting. Additionally, the constituents of the linker can influence the catalytic activity of proteins it is fusing, so what linker to use is a key consideration in designing fusion proteins.
Design Notes
Codon-optimised for expression in E. coli
References
Li G, Huang Z, Zhang C, Dong BJ, Guo RH, Yue HW, et al. Construction of a linker library with widely controllable flexibility for fusion protein design. Appl Microbiol Biotechnol. 2016;100(1):215-25.
Ceballos-Alcantarilla E, Merkx M. Understanding and applications of Ser/Gly linkers in protein engineering. Methods Enzymol. 2021;647:1-22.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
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