Ontology highlight
ABSTRACT:
SUBMITTER: Alegre-Cebollada J
PROVIDER: S-EPMC2025675 | biostudies-literature | 2007 Nov
REPOSITORIES: biostudies-literature
Alegre-Cebollada Jorge J Martínez del Pozo Alvaro A Gavilanes José G JG Goormaghtigh Erik E
Biophysical journal 20070615 9
The structure of the actinoporin sticholysin II (StnII) in the pore state was investigated by Fourier transform infrared spectroscopy in the attenuated total reflection configuration. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/cholesterol unilamellar vesicles were employed. The alpha-helix content increases in approximately 30% upon lipid binding, which agrees with an extension of eight or nine residues at the N-terminal helix. Furthermore, analyses of dichroic spectra show that the extend ...[more]