Journal article

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

University of Melbourne Researchers