Difference between revisions of "Part:BBa J176131"

Revision as of 16:30, 8 March 2012

PLrigid

(EAAAR)4 peptide linker, rigid; alpha helix secondary structure

Usage and Biology

PLrigid is a 20 a.a. peptide that is based on a previously characterized alpha-helix motif (EAAAR) (Merutka et al., 1991; Sommese et al., 2010). This BioBrick part is based on work reported by Yan et al., 2007, where they used this motif to build transcription factors with tandem DNA binding domains spaced apart by rigid linkers. 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 in space.

REFERENCES

Merutka G, Shalongo W, Stellwagen E. (1991) A model peptide with enhanced helicity. Biochem. 30: 4245-4248.
Sommese RF, Sivaramakrishnan S, Baldwin RL, Spudich JA. (2010) Helicity of short E-R/K peptides. Protein Sci. 19: 2001-2005.
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:

10
INCOMPATIBLE WITH RFC[10]
Illegal PstI site found at 20
Illegal PstI site found at 35
12
INCOMPATIBLE WITH RFC[12]
Illegal PstI site found at 20
Illegal PstI site found at 35
21
COMPATIBLE WITH RFC[21]
23
INCOMPATIBLE WITH RFC[23]
Illegal PstI site found at 20
Illegal PstI site found at 35
25
INCOMPATIBLE WITH RFC[25]
Illegal PstI site found at 20
Illegal PstI site found at 35
1000
COMPATIBLE WITH RFC[1000]

@@ Line 7: / Line 7: @@
 ===Usage and Biology===
-PLrigid is a 20 a.a. 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>
+PLrigid is a 20 a.a. peptide that is based on a previously characterized alpha-helix motif (EAAAR) (Merutka et al., 1991; Sommese et al., 2010). This BioBrick part is based on work reported by Yan et al., 2007, where they used this motif to build transcription factors with tandem DNA binding domains spaced apart by rigid linkers. 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 in space.<br>
 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
+# Merutka G, Shalongo W, Stellwagen E. (1991) A model peptide with enhanced helicity. Biochem. 30: 4245-4248.
+# Sommese RF, Sivaramakrishnan S, Baldwin RL, Spudich JA. (2010) Helicity of short E-R/K peptides. Protein Sci. 19: 2001-2005.
+# 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.