Difference between revisions of "Part:BBa K4375010"
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<partinfo>BBa_K4375010 short</partinfo> | <partinfo>BBa_K4375010 short</partinfo> | ||
− | A 13 amino acid | + | A 13 amino acid long GS linker (Glycine-Serine linker), which gives the possibility of a flexible linkage between protein domains. |
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− | + | <html> | |
+ | </p> | ||
+ | </html> | ||
+ | __TOC__ | ||
+ | ==Usage and Biology== | ||
+ | The GS linker is a flexible linker that can connect different protein domains or regions. This stretch is rich in serine and glycine amino acids and thus provides high mobility to the protein regions conjugated to it. GS linkers are usually useful in connecting antibody fragments to achieve better antigen binding or improve protein folding. | ||
− | + | ||
− | + | ==Sequence and Features== | |
<partinfo>BBa_K4375010 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4375010 SequenceAndFeatures</partinfo> | ||
+ | |||
+ | ==Reference== | ||
+ | Chen, X.; Zaro, J. L.; Shen, W.-C. Fusion Protein Linkers: Property, Design and Functionality. Advanced Drug Delivery Reviews 2013, 65 (10), 1357–1369. https://doi.org/10.1016/j.addr.2012.09.039. | ||
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Latest revision as of 16:21, 10 October 2022
13 aa long GS-linker
A 13 amino acid long GS linker (Glycine-Serine linker), which gives the possibility of a flexible linkage between protein domains.
Usage and Biology
The GS linker is a flexible linker that can connect different protein domains or regions. This stretch is rich in serine and glycine amino acids and thus provides high mobility to the protein regions conjugated to it. GS linkers are usually useful in connecting antibody fragments to achieve better antigen binding or improve protein folding.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
Chen, X.; Zaro, J. L.; Shen, W.-C. Fusion Protein Linkers: Property, Design and Functionality. Advanced Drug Delivery Reviews 2013, 65 (10), 1357–1369. https://doi.org/10.1016/j.addr.2012.09.039.