Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides.

@article{Pukala2004InvestigatingTI,
  title={Investigating the importance of the flexible hinge in caerin 1.1: solution structures and activity of two synthetically modified caerin peptides.},
  author={Tara Pukala and Craig S Brinkworth and John A Carver and John H. Bowie},
  journal={Biochemistry},
  year={2004},
  volume={43 4},
  pages={937-44}
}
Caerin 1.1 is a potent broad-spectrum antibacterial peptide isolated from a number of Australian frogs of the Litoria genus. In membrane-like media, this peptide adopts two alpha-helices, separated by a flexible hinge region bounded by Pro15 and Pro19. Previous studies have suggested that the hinge region is important for effective orientation of the two helices within the bacterial cell membrane, resulting in lysis via the carpet mechanism. To evaluate the importance of the two Pro residues… CONTINUE READING

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