Solid-state NMR and simulation studies of equinatoxin II N-terminus interaction with lipid bilayers
Yuen Han Lam, Andrew Hung, Raymond S Norton, Frances Separovic, Anthony Watts
Proteins - Structure, Function, and Bioinformatics | WILEY | Published : 2010
The interaction with model membranes of a peptide, EqtII(1-32), corresponding to the N-terminal region of the pore-forming toxin equinatoxin II (EqtII) has been studied using solid-state NMR and molecular dynamics (MD) simulations. The distances between specifically labeled nuclei in [(19)F-para]Phe16-[1-(13)C]Leu19 and [(19)F-para]Phe16-[(15)N]Leu23 analogs of EqtII(1-32) measured by REDOR in lyophilized peptide were in agreement with published crystal and solution structures. However, in both DMPC and mixed DMPC:SM membrane environments, significant changes in the distances between the labeled amino acid pairs were observed, suggesting changes in helical content around the experimentally s..View full abstract
Awarded by Engineering and Physical Sciences Research Council
Grant sponsors: The Medical Research Council (UK); The Australian Research Council.