Difference between revisions of "Part:BBa J176131"
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | PLrigid is a short peptide that has an alpha-helix structure. We use it as a "linker" to connect protein domains/ modules. Alpha helices are thought to be rigid structures that restrict the position of one end relative to the other. Lack of "bendability" keeps the two proteins attached at either end from coming closer together. Since the proteins are also unable to move farther apart when they are attached with a rigid linker, the relative position of the two proteins is fixed. | + | PLrigid is a short peptide that has an alpha-helix structure. This part is based on the design reported by Yan et al., 2007. We use it as a "linker" to connect protein domains/ modules. Alpha helices are thought to be rigid structures that restrict the position of one end relative to the other. Lack of "bendability" keeps the two proteins attached at either end from coming closer together. Since the proteins are also unable to move farther apart when they are attached with a rigid linker, the relative position of the two proteins is fixed.<br> |
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+ | REFERENCES | ||
+ | # Yan W, Imanishi M, Futaki S, Sugiura Y. (2007) alpha-Helical Linker of an Artificial 6-Zinc Finger Peptide Contributes to Selective DNA Binding to a Discontinuous Recognition Sequence. Biochem. 46: 8517-8524 | ||
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Revision as of 22:00, 7 March 2012
PLrigid
(EAAAR)4 peptide linker, rigid; alpha helix secondary structure
Usage and Biology
PLrigid is a short peptide that has an alpha-helix structure. This part is based on the design reported by Yan et al., 2007. We use it as a "linker" to connect protein domains/ modules. Alpha helices are thought to be rigid structures that restrict the position of one end relative to the other. Lack of "bendability" keeps the two proteins attached at either end from coming closer together. Since the proteins are also unable to move farther apart when they are attached with a rigid linker, the relative position of the two proteins is fixed.
REFERENCES
- Yan W, Imanishi M, Futaki S, Sugiura Y. (2007) alpha-Helical Linker of an Artificial 6-Zinc Finger Peptide Contributes to Selective DNA Binding to a Discontinuous Recognition Sequence. Biochem. 46: 8517-8524
Sequence and Features
Assembly Compatibility:
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 20
Illegal PstI site found at 35 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 20
Illegal PstI site found at 35 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 20
Illegal PstI site found at 35 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 20
Illegal PstI site found at 35 - 1000COMPATIBLE WITH RFC[1000]