Khattari, Ziad

[["dc.bibliographiccitation.firstpage","3402"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry B"],["dc.bibliographiccitation.lastpage","3407"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Khattari, Z."],["dc.contributor.author","Ruschel, Y."],["dc.contributor.author","Wen, H. Z."],["dc.contributor.author","Fischer, A."],["dc.contributor.author","Fischer, T. M."],["dc.date.accessioned","2018-11-07T11:17:37Z"],["dc.date.available","2018-11-07T11:17:37Z"],["dc.date.issued","2005"],["dc.description.abstract","The surface shear viscosity of a myelin mimetic Langmuir monolayer is investigated upon adsorption of myelin basic protein (MBP). We measure an increase of the surface shear viscosity at picomolar concentrations of the protein, suggesting that the globular conformation of MBP changes upon adsorption at the monolayer. The conformational change enables hydrodynamic interactions of the proteins, with a typical separation of hundreds of nanometers. This unfolding is essential for the compactification of the myelin sheath, serving an enhanced saltatory signal transduction in vertebrates. The viscometry used extends the sensitivity of standard surface viscometers toward lower viscosities."],["dc.identifier.doi","10.1021/jp045493z"],["dc.identifier.isi","000227247100047"],["dc.identifier.pmid","16851371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54848"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1520-6106"],["dc.title","Compactification of a myelin mimetic Langmuir monolayer upon adsorption and unfolding of myelin basic protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","769"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","779"],["dc.bibliographiccitation.volume","341"],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Akkawi, M"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Arkin, I. T."],["dc.date.accessioned","2017-09-07T11:43:16Z"],["dc.date.available","2017-09-07T11:43:16Z"],["dc.date.issued","2004"],["dc.description.abstract","The agent responsible for the recent severe acute respiratory syndrome (SARS) outbreak is a previously unidentified coronavirus. While there is a wealth of epidemiological studies, little if any molecular characterization of SARS coronavirus (SCoV) proteins has been carried out. Here we describe the molecular characterization of SCoV E protein, a critical component of the virus responsible for virion envelope morphogenesis. We conclusively show that SCoV E protein contains an unusually short, palindromic transmembrane helical hairpin around a previously unidentified pseudo-center of symmetry, a structural feature which seems to be unique to SCoV The hairpin deforms lipid bilayers by way of increasing their curvature, providing for the first time a molecular explanation of E protein's pivotal role in viral budding. The molecular understanding of this critical component of SCoV may represent the beginning of a concerted effort aimed at inhibiting its function, and consequently, viral infectivity. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2004.06.044"],["dc.identifier.gro","3143955"],["dc.identifier.isi","000223240200010"],["dc.identifier.pmid","15288785"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1526"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0022-2836"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","membrane biophysics"],["dc.title","A highly unusual palindromic transmembrane helical hairpin formed by SARS coronavirus E protein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","41"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Biomembranes"],["dc.bibliographiccitation.lastpage","50"],["dc.bibliographiccitation.volume","1848"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Koehler, Sebastian"],["dc.contributor.author","Xu, Yihui"],["dc.contributor.author","Aeffner, Sebastian"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","We have investigated the structure and interaction of solid-supported multilamellar phospholipid bilayers in view of stalk formation as model systems for membrane fusion. The multi-component bilayers were composed of ternary and quaternary mixtures, containing phosphatidylcholines, phosphatidylethanolamines, sphingomyelin, cholesterol, diacylglycerol, and phosphatidylinositol. Analysis of the obtained electron density profiles and the pressure-distance curves reveals systematic changes in structure and hydration repulsion. The osmotic pressure needed to induce stalk formation at the transition from the fluid lamellar to the rhombohedral phase indicates how membrane fusion properties are modified by bilayer composition. (C) 2014 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamem.2014.08.010"],["dc.identifier.gro","3141990"],["dc.identifier.isi","000347509200006"],["dc.identifier.pmid","25261611"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3323"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft (DFG)"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","0006-3002"],["dc.relation.issn","0005-2736"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Stalk formation as a function of lipid composition studied by X-ray reflectivity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","34"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.lastpage","38"],["dc.bibliographiccitation.volume","357"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Metzger, T. H."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:54:32Z"],["dc.date.available","2017-09-07T11:54:32Z"],["dc.date.issued","2005"],["dc.description.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. (C) 2004 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.physb.2004.11.015"],["dc.identifier.gro","3143885"],["dc.identifier.isi","000227309100008"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1448"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.publisher.place","Amsterdam"],["dc.relation.eissn","1873-2135"],["dc.relation.eventlocation","Bad Honnef, GERMANY"],["dc.relation.ispartof","Physica B: Condensed Matter"],["dc.relation.issn","0921-4526"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","SARS E protein in phospholipid bilayers: an anomalous X-ray reflectivity study"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","563"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","571"],["dc.bibliographiccitation.volume","89"],["dc.contributor.author","Manor, J."],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Arkin, I. T."],["dc.date.accessioned","2017-09-07T11:54:24Z"],["dc.date.available","2017-09-07T11:54:24Z"],["dc.date.issued","2005"],["dc.description.abstract","Linear dichroism, the unequal absorption of parallel and perpendicular linear polarized light, is often used to determine the anisotropic ordering of rodlike polymers in a smectic phase, such as helices in a lipid bilayer. It is a measure of two properties of the sample: 1), orientation of the chromophore transition dipole moment (TDM) and 2), disorder. Since it is the orientation of the chromophore TDM that is needed for high resolution structural studies, it is imperative to either deconvolve sample disorder, or at a minimum, estimate its effect upon the calculated TDM orientation. Herein, a rigorous analysis of the effects of disorder is undertaken based on the recently developed Gaussian disorder model implemented in linear dichroism data. The calculation of both the rod tilt and rotational pitch angles as a function of the disorder and dichroism, yield the following conclusions: Disorders smaller than 5 degrees have a vanishingly small effect on the calculated polymer orientation, whereas values smaller than 10 degrees have a negligible effect on the calculated parameters. Disorders larger than 10 degrees have an appreciable effect on the calculated orientational parameters and as such must be estimated before any structural characterization. Finally the theory is tested on the HIV vpu transmembrane domain, employing experimental mosaicity measurements from x-ray reflectivity rocking scans and linear dichroism."],["dc.identifier.doi","10.1529/biophysj.104.058842"],["dc.identifier.gro","3143826"],["dc.identifier.isi","000230114500057"],["dc.identifier.pmid","15834005"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1383"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Disorder influence on linear dichroism analyses of smectic phases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21772"],["dc.bibliographiccitation.issue","46"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry B"],["dc.bibliographiccitation.lastpage","21778"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Muruganathan, R. M."],["dc.contributor.author","Khattari, Z."],["dc.contributor.author","Fischer, T. M."],["dc.date.accessioned","2018-11-07T10:54:09Z"],["dc.date.available","2018-11-07T10:54:09Z"],["dc.date.issued","2005"],["dc.description.abstract","We investigate the nonequilibrium behavior of two-dimensional gas bubbles in Langmuir monolayers. A cavitation bubble is induced in liquid expanded phase by locally heating a Langmuir monolayer with an IR-laser. At low IR-laser power the cavitation bubble is immersed in quiescent liquid expanded monolayer. At higher IR-laser power thermo capillary flow around the laser-induced cavitation bubble sets in. The thermo capillary flow is caused by a temperature dependence of the gas/liquid line tension. The slope of the line tension with temperature is determined by measuring the thermo capillary flow velocity. Thermodynamically stable satellite bubbles are generated by increasing the surface area of the monolayer. Those satellite bubbles collide with the cavitation bubble. Upon collision the satellite bubbles either coalesce with the cavitation bubble or slide past the cavitation bubble. Moreover we show that the satellite bubbles can also be produced by the emission from the laser-induced cavitation bubbles."],["dc.identifier.doi","10.1021/jp0537714"],["dc.identifier.isi","000233437100045"],["dc.identifier.pmid","16853828"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/49504"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","1520-6106"],["dc.title","Nonequilibrium bubbles in a flowing Langmuir monolayer"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2336"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","2343"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Kuesel, Andrea"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Banerjee, Arnab"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:49:23Z"],["dc.date.available","2017-09-07T11:49:23Z"],["dc.date.issued","2007"],["dc.description.abstract","Peptides with alternating amino acid configuration provide helical secondary structures that are especially known from the membrane channel and pore-forming gramicidin A. In analogy to this natural D,L-alternating pentadecapeptide, the potential of D,L-alternating peptides for membrane insertion is investigated using the model dodecamer peptide H-(Phe-Tyr)(5)-Trp-Trp-OH. This aromatic peptide is introduced as a novel pore-forming synthetic analogue of gramicidin A. It forms a well-organized homodimer similar to one of the gromicidin A transmembrane motifs."],["dc.identifier.doi","10.1002/cphc.200700477"],["dc.identifier.gro","3143411"],["dc.identifier.isi","000251004200007"],["dc.identifier.pmid","17935092"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/922"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1439-4235"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","membrane biophysics"],["dc.title","Conformation and interaction of a D,L-alternating peptide with a bilayer membrane: X-ray reflectivity, CD, and FTIR spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","45"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","55"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Khattari, Z."],["dc.contributor.author","Arbely, E."],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Salditt, T."],["dc.date.accessioned","2017-09-07T11:49:54Z"],["dc.date.available","2017-09-07T11:49:54Z"],["dc.date.issued","2006"],["dc.description.abstract","We have investigated the effect of the transmembrane domain of three viral ion channel proteins on the lipid bilayer structure by X-ray reflectivity and scattering from oriented planar bilayers. The proteins show a similar effect on the lipid bilayer structural parameters: an increase in the lipid bilayer hydrophobic core, a decrease in the amplitude of the vertical density profile and a systematic change in the ordering of the acyl chains as a function of protein-to-lipid ratio. These results are discussed in a comparative view."],["dc.identifier.doi","10.1007/s00249-006-0099-x"],["dc.identifier.gro","3143578"],["dc.identifier.isi","000241897800005"],["dc.identifier.pmid","17019591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1107"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0175-7571"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Viral ion channel proteins in model membranes: a comparative study by X-ray reflectivity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2038"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2050"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Khattari, Ziad"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Akkawi, M."],["dc.contributor.author","Arbely, E"],["dc.contributor.author","Arkin, I. T."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:53:20Z"],["dc.date.available","2017-09-07T11:53:20Z"],["dc.date.issued","2006"],["dc.description.abstract","We investigated the structure of the hydrophobic domain of the severe acute respiratory syndrome E protein in model lipid membranes by x-ray reflectivity and x-ray scattering. In particular, we used x-ray reflectivity to study the location of an iodine-labeled residue within the lipid bilayer. The label imposes spatial constraints on the protein topology. Experimental data taken as a function of protein/lipid ratioP/L and different swelling states support the hairpin conformation of severe acute respiratory syndrome E protein reported previously. Changes in the bilayer thickness and acyl-chain ordering are presented as a function of P/L, and discussed in view of different structural models."],["dc.identifier.doi","10.1529/biophysj.105.072892"],["dc.identifier.gro","3143728"],["dc.identifier.isi","000235709500017"],["dc.identifier.pmid","16361349"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1274"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0006-3495"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","SARS coronavirus E protein in phospholipid bilayers: An X-ray study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]