Tachyplesin: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The amino acid sequence of the TPI is NH₂-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-CONH₂. | The amino acid sequence of the TPI is NH₂-Lys-Trp-Cys-Phe-Arg-Val-Cys-Tyr-Arg-Gly-Ile-Cys-Tyr-Arg-Arg-Cys-Arg-CONH₂. | ||
It adopts antiparallel β-sheet (hairpin) conformation in solution stabilized by | It adopts antiparallel β-sheet (hairpin) conformation in solution stabilized by two cross-strand <scene name='67/671725/Disulfide_bonds/1'> disulfide bonds </scene> between Cys³-Cys¹⁶ and Cys⁷-Cys¹², and its [http://en.wikipedia.org/wiki/Protein_primary_structure C-terminus is amidated].<ref name=Laederach>PMID:12369825</ref><ref name=Kushibiki>PMID:24389234</ref> | ||
[[Image:scheme.jpg]] | [[Image:scheme.jpg]] | ||
Tachyplesin is highly stable at low pH and high temperature. This stability seems to be due to the rigid structure imposed by the two disulfid linkage. | |||
Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | Besides, there exists H-bond and aromatic ring stacking interactions which helps stabilizing the hairpin loop structure of the peptide. | ||
