| Título: | Infrared spectroscopy study on the conformational changes leading to pore formation of the toxin Sticholysin II |
| Autores: | Alegre Cebollada, Jorge ; Martínez del Pozo, Álvaro ; Gavilanes, José G. ; Goormaghtigh, Erik |
| Tipo de documento: | texto impreso |
| Fecha de publicación: | 2007-11 |
| Dimensiones: | application/pdf |
| Nota general: | info:eu-repo/semantics/openAccess |
| Idiomas: | |
| Palabras clave: | Estado = Publicado , Materia = Ciencias: Química: Bioquímica , Tipo = Artículo |
| Resumen: |
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 a-helix content increases in;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 extended N-terminal helix would have a 31º tilt with respect to the membrane normal. The orientation of the central beta-sandwich was also estimated. In addition, it was detected that StnII alters the orientation of the lipid acyl chains. 1H/2Hexchange experiments sustain a mainly superficial interaction between StnII and the membrane, with no protection of the beta-sandwich. The implications of the results in the mechanism of pore formation are discussed. |
| En línea: | https://eprints.ucm.es/id/eprint/7616/1/AlegreCebollada2007b.pdf |
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