Difference between revisions of "Part:BBa K4144009"
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===Usage and Biology=== | ===Usage and Biology=== | ||
Linkers can be classified into three groups: flexible, rigid and cleavable. Flexible linkers are generally composed of small, non-polar or polar residues such as Gly, Ser and Thr. The most common is the (Gly4Ser)n linker (Gly–Gly–Gly–Gly–Ser)n, where n indicates the number of repeats of the motif. Polyglycine linkers have also been evaluated, but the addition of a polar residue such as serine can reduce linker–protein interactions and preserve protein function. Due to their flexibility, these linkers are unstructured and thus provided limited domain separation in a previous study.<br> | Linkers can be classified into three groups: flexible, rigid and cleavable. Flexible linkers are generally composed of small, non-polar or polar residues such as Gly, Ser and Thr. The most common is the (Gly4Ser)n linker (Gly–Gly–Gly–Gly–Ser)n, where n indicates the number of repeats of the motif. Polyglycine linkers have also been evaluated, but the addition of a polar residue such as serine can reduce linker–protein interactions and preserve protein function. Due to their flexibility, these linkers are unstructured and thus provided limited domain separation in a previous study.<br> |
Revision as of 02:51, 12 October 2022
A linker between protein of interest and tag
Usage and Biology
Linkers can be classified into three groups: flexible, rigid and cleavable. Flexible linkers are generally composed of small, non-polar or polar residues such as Gly, Ser and Thr. The most common is the (Gly4Ser)n linker (Gly–Gly–Gly–Gly–Ser)n, where n indicates the number of repeats of the motif. Polyglycine linkers have also been evaluated, but the addition of a polar residue such as serine can reduce linker–protein interactions and preserve protein function. Due to their flexibility, these linkers are unstructured and thus provided limited domain separation in a previous study.
Reference
[1] Mart Krupovicˇ and Dennis H. Bamford. Holin of bacteriophage lambda: structural insights into a membrane lesion. Molecular Microbiology(2008)69(4), 781–783.
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]