Tachyplesin: Difference between revisions
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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. | 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.<ref name=Nakamura></ref> | ||
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. | ||
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</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
Nakamura, Takanori, et al. "Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure." Journal of Biological Chemistry 263.32 (1988): 16709-16713. | |||
<references/> | <references/> | ||
