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

Z. Khattari; G. Brotons; E. Arbely; I. T. Arkin; T. H. Metzger; T. Salditt

doi:10.1016/j.physb.2004.11.015

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

Z. Khattari
, G. Brotons
, E. Arbely
, I. T. Arkin
, T. H. Metzger
, T. Salditt^*

^*Corresponding author for this work

Department of Biological Chemistry

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

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.

Original language	English
Pages (from-to)	34-38
Number of pages	5
Journal	Physica B: Condensed Matter
Volume	357
Issue number	1-2 SPEC. ISS.
DOIs	https://doi.org/10.1016/j.physb.2004.11.015
State	Published - 28 Feb 2005

Bibliographical note

Funding Information:
Financial support by the DFG through the German–Israel–Palestine trilateral Project SA 7772/6-1 is gratefully acknowledged. We thank the team of ESRF/ID1 for the continuous help during the experiment and T. Schülli for helpful discussions.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

Anomalous scattering
Lipid-peptide interaction
SARS E protein

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10.1016/j.physb.2004.11.015

Cite this

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title = "SARS E protein in phospholipid bilayers: An anomalous X-ray reflectivity study",

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.",

keywords = "Anomalous scattering, Lipid-peptide interaction, SARS E protein",

author = "Z. Khattari and G. Brotons and E. Arbely and Arkin, \{I. T.\} and Metzger, \{T. H.\} and T. Salditt",

note = "Funding Information: Financial support by the DFG through the German–Israel–Palestine trilateral Project SA 7772/6-1 is gratefully acknowledged. We thank the team of ESRF/ID1 for the continuous help during the experiment and T. Sch{\"u}lli for helpful discussions.",

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T2 - An anomalous X-ray reflectivity study

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AU - Brotons, G.

AU - Arbely, E.

AU - Arkin, I. T.

AU - Metzger, T. H.

AU - Salditt, T.

N1 - Funding Information: Financial support by the DFG through the German–Israel–Palestine trilateral Project SA 7772/6-1 is gratefully acknowledged. We thank the team of ESRF/ID1 for the continuous help during the experiment and T. Schülli for helpful discussions.

PY - 2005/2/28

Y1 - 2005/2/28

N2 - 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.

AB - 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.

KW - Anomalous scattering

KW - Lipid-peptide interaction

KW - SARS E protein

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ER -

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

Abstract

Bibliographical note

UN SDGs

Keywords

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