Part:BBa_J176131
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
- 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]
function | protein linker |