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

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About: SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study
Creator	Arbely, E Arkin, I Brotons, G Khattari, Z Salditt, T Metzger, T
Source	Elsevier; Medline; PMC
abstract	Abstract 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.
has issue date	2005-02-28(xsd:dateTime)
bibo:doi	10.1016/j.physb.2004.11.015
bibo:pmid	32288217
has license	els-covid
sha1sum (hex)	9f1bc99798e8823e690697394dcb23533a45c60e
schema:url	https://doi.org/10.1016/j.physb.2004.11.015
resource representing a document's title	SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study
has PubMed Central identifier	PMC7127356
has PubMed identifier	32288217
schema:publication	Physica B: Condensed Matter
resource representing a document's body	covid:9f1bc99798e8823e690697394dcb23533a45c60e#body_text
is schema:about of	named entity 'SARS' named entity 'Fourier synthesis' named entity 'X-ray reflectivity' named entity 'FORM' named entity 'STUDY' named entity 'PROTEIN ' named entity 'ANOMALOUS' named entity 'X-RAY REFLECTIVITY' named entity 'EXPERIMENTAL' named entity 'E PROTEIN' named entity 'DEPOSITED' named entity 'STUDY' named entity 'ANOMALOUS' named entity 'SARS' named entity 'PHOSPHOLIPID' named entity 'HERE' named entity 'SURFACES' named entity 'RESPECT' named entity 'DMPC' named entity 'ASSOCIATED WITH' named entity 'E PROTEIN' named entity 'ELECTRON DENSITY' named entity 'DISCUSS' named entity 'OUR' named entity 'EXPERIMENTS' named entity 'PHOSPHOLIPID' named entity 'DERIVED' named entity 'MEMBRANES' named entity 'SYNTHESIS' named entity 'IODINE-' named entity 'SILICON' named entity 'LIPID BILAYER' named entity 'PROFILE' named entity 'AIM' named entity 'PROTEIN ' named entity 'DIFFICULTIES' named entity 'PHENYLALANINE' named entity 'ANALYSIS' named entity 'FOURIER' named entity 'TO LOCALIZE' named entity 'X-RAY REFLECTIVITY' named entity 'IMPORTANT' named entity 'RESIDUE' named entity 'MEMBRANE PROTEIN' named entity 'PEPTIDE CONFORMATION' named entity 'REPORT' named entity 'peptide' named entity 'phospholipid' named entity 'Fourier synthesis' named entity 'SARS' named entity 'X-ray reflectivity' named entity 'silicon' named entity 'phospholipid bilayers' named entity 'X-ray reflectivity' named entity 'study' named entity 'reflectivity' named entity 'Bragg peak' named entity 'lipid membranes' named entity 'monochromator' named entity 'lipid bilayers' named entity 'iodine' named entity 'SARS' named entity 'Bragg' named entity 'vapor-pressure' named entity 'self-assemble' named entity 'lamellar' named entity 'electron density' named entity 'scattering' named entity 'iodine' named entity 'hydrophobic' named entity 'photon energies' named entity 'thermal fluctuations' named entity 'monochromator' named entity 'multilamellar' named entity 'biomedical research' named entity 'dispersion'

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