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SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study

We report on an anomalous X-ray reflectivity study to locate a labelled residue of a membrane protein with respect to the lipid bilayer. From such experiments, important constraints on the protein or peptide conformation can be derived. Specifically, our aim is to localize an iodine-labelled phenyla...

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Detalles Bibliográficos
Autores principales: Khattari, Z., Brotons, G., Arbely, E., Arkin, I.T., Metzger, T.H., Salditt, T.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier B.V. 2005
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7127356/
https://www.ncbi.nlm.nih.gov/pubmed/32288217
http://dx.doi.org/10.1016/j.physb.2004.11.015
Descripción
Sumario:We report on an anomalous X-ray reflectivity study to locate a labelled residue of a membrane protein with respect to the lipid bilayer. From such experiments, important constraints on the protein or peptide conformation can be derived. Specifically, our aim is to localize an iodine-labelled phenylalanine in the SARS E protein, incorporated in DMPC phospholipid bilayers, which are deposited in the form of thick multilamellar stacks on silicon surfaces. Here, we discuss the experimental aspects and the difficulties associated with the Fourier synthesis analysis that gives the electron density profile of the membranes.