Difference between revisions of "Part:BBa K1486004"
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===Usage and Biology=== | ===Usage and Biology=== | ||
This linker is part of the group of flexible ligands composed of small, non-polar amino acids such as Gly and polar such as Ser. In this way, they guarantee high mobility and offer flexibility for the functional domains of connection. Studies show that when proline residues are exchanged in place of terminal glycine residues, degrees of independence are lost (Ruiz et al., 2016b). In this way, enzyme activity is decreased, which leads to low catalytic efficiencies. We can conclude that flexible ligands provide a reduced catalytic activity for proteins. | This linker is part of the group of flexible ligands composed of small, non-polar amino acids such as Gly and polar such as Ser. In this way, they guarantee high mobility and offer flexibility for the functional domains of connection. Studies show that when proline residues are exchanged in place of terminal glycine residues, degrees of independence are lost (Ruiz et al., 2016b). In this way, enzyme activity is decreased, which leads to low catalytic efficiencies. We can conclude that flexible ligands provide a reduced catalytic activity for proteins. | ||
| − | + | <br> | |
| + | The article “Linkers: a synergistic way for chimeric proteins, 2020”, talks about the constitution and interaction of the flexible linker (Gly-Gly-Gly-Gly-Ser)n, where “n” specifies the sum of the repetitions of the residue. These linkers provide partial domain separation. It is possible to observe that the amount of Gly, Ser and Thr residues results in flexibility that allows the | ||
mobility of the functional binding domains. | mobility of the functional binding domains. | ||
Latest revision as of 08:27, 21 October 2021
flexible linker 2x (GGGGS)
Flexible linker used to fuse two proteins.
Usage and Biology
This linker is part of the group of flexible ligands composed of small, non-polar amino acids such as Gly and polar such as Ser. In this way, they guarantee high mobility and offer flexibility for the functional domains of connection. Studies show that when proline residues are exchanged in place of terminal glycine residues, degrees of independence are lost (Ruiz et al., 2016b). In this way, enzyme activity is decreased, which leads to low catalytic efficiencies. We can conclude that flexible ligands provide a reduced catalytic activity for proteins.
The article “Linkers: a synergistic way for chimeric proteins, 2020”, talks about the constitution and interaction of the flexible linker (Gly-Gly-Gly-Gly-Ser)n, where “n” specifies the sum of the repetitions of the residue. These linkers provide partial domain separation. It is possible to observe that the amount of Gly, Ser and Thr residues results in flexibility that allows the
mobility of the functional binding domains.
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]
Functional Parameters
| chassis | E coli |
| device_type | linker |
| direction | forward |
Isoelectric Point: 5,52 Molecular Weight: 648,59Da
References
- Michela S, Baenziger-Tobler N, Wibke L, Sarah B, Julian B, Dragan G. Linker Length Matters, Fynomer-Fc Fusion with an Optimized Linker Displaying Picomolar IL-17A Inhibition Potency. IMMUNOLOGY| VOLUME 289, ISSUE 20, P14392-14398, MAY 2014