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

Abstract

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..

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University of Melbourne Researchers