Salditt, Tim

[["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","992"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Europhysics Letters (EPL)"],["dc.bibliographiccitation.lastpage","998"],["dc.bibliographiccitation.volume","75"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Belloni, L."],["dc.contributor.author","Zemb, Th."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:52:35Z"],["dc.date.available","2017-09-07T11:52:35Z"],["dc.date.issued","2006"],["dc.description.abstract","We have investigated the structure, fluctuations and elasticity parameters of charged fluid membranes composed of didodecyldimethylammonium halide bilayers (DDAX) with different counterions (X = Cl- or Br-) by non-specular (diffuse) X-ray scattering. The samples have been prepared as highly aligned thick stacks on silicon support and have been swollen at controlled osmotic pressures. From line-shape analysis of the diffuse scattering, we can determine the fluctuation amplitudes of the membranes in the L-alpha phase and the characteristic correlation lengths. According to the Caille model, the measured structural parameters have been expressed in terms of the exponent eta and smectic penetration length.lambda from which the smectic compression modulus B (J/m(3)) and the bending modulus K (J/m) have been determined, as a function of the swelling state. We show that the results are in quantitative agreement with the mean-field electrostatic Poisson-Boltzmann calculations, controlled by the bilayers surface charge density (surfactant head groups with free or condensed counterions)."],["dc.identifier.doi","10.1209/epl/i2006-10207-5"],["dc.identifier.gro","3143632"],["dc.identifier.isi","000241491200023"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1167"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0295-5075"],["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","Elasticity of fluctuating charged membranes probed by X-ray grazing-incidence diffuse scattering"],["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","61"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.lastpage","65"],["dc.bibliographiccitation.volume","357"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Constantin, Doru"],["dc.contributor.author","Madsen, Anders"],["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","Charged surfactant bilayers deposited in thick multilayer films and swollen in vapor or in solution have been studied by coherent X-ray scattering. We report a pronounced static speckle pattern which persists under conditions of full hydration, despite the fact that the bilayers are fluid, relatively soft, and consisting of soluble amphiphiles (DDABr). Characteristic of the macroscopic domains size, the speckle pattern is observed in the plane of incidence (rocking curves). Contrarily, out-of-plane scans, which probe smaller lateral distances along the multilayer, exhibit a smooth diffuse scattering curve characteristic of thermal fluctuations of membranes. (C) 2004 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.physb.2004.11.020"],["dc.identifier.gro","3143888"],["dc.identifier.isi","000227309100013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1451"],["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.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","Coherent X-ray scattering and speckle pattern of solid-supported multilayers of surfactant bilayers"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","97"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.lastpage","109"],["dc.bibliographiccitation.volume","303"],["dc.contributor.author","Qu, Dan"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Bosio, Vera"],["dc.contributor.author","Fery, Andreas"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Langevin, Dominique"],["dc.contributor.author","von Klitzing, Regine"],["dc.date.accessioned","2017-09-07T11:49:26Z"],["dc.date.available","2017-09-07T11:49:26Z"],["dc.date.issued","2007"],["dc.description.abstract","The paper gives an overview on interactions between two opposing interfaces in liquids. The interfaces are either solid (two silica surfaces) or fluid (in foam films or in membrane stacks). The liquids are either simple ones (water or salty water) or contain polyelectrolytes. In the latter case, the confinement leads to a structuring of the polyelectrolytes which leads to oscillatory forces in addition to DLVO forces. The effect of interface properties on the interactions is studied by modification of interfaces. In case of solid interfaces, they are modified by the adsorption of polyelectrolyte multilayers, while fluid interfaces are varied by changing the amphiphile/polymer combination. With regard to the studied problem, different methods are used to study the interactions. (c) 2007 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.colsurfa.2007.03.055"],["dc.identifier.gro","3143457"],["dc.identifier.isi","000247771200011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/973"],["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.conference","French/ German Network on Complex Fluids - From 2D to 3D"],["dc.relation.eissn","1873-4359"],["dc.relation.eventlocation","Paris, FRANCE"],["dc.relation.ispartof","Colloids and Surfaces A: Physicochemical and Engineering Aspects"],["dc.relation.issn","0927-7757"],["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","Interactions across liquid thin films"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3978"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","3987"],["dc.bibliographiccitation.volume","92"],["dc.contributor.author","Constantin, Doru"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Jarre, A."],["dc.contributor.author","Li, C."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:49:28Z"],["dc.date.available","2017-09-07T11:49:28Z"],["dc.date.issued","2007"],["dc.description.abstract","We have investigated the x-ray scattering signal of highly aligned multilayers of the zwitterionic lipid 1,2-dimyristoylsnglycero-3-phosphatidylcholine containing pores formed by the antimicrobial peptide alamethicin as a function of the peptide/lipid ratio. We are able to obtain information on the structure factor of the pore fluid, which then yields the interaction potential between pores in the plane of the bilayers. Aside from a hard core with a radius corresponding to the geometric radius of the pore, we find a repulsive lipid-mediated interaction with a range of similar to 30 angstrom and a contact value of 2.4 k(B)T. This result is in qualitative agreement with recent theoretical models."],["dc.identifier.doi","10.1529/biophysj.106.101204"],["dc.identifier.gro","3143486"],["dc.identifier.isi","000246401800022"],["dc.identifier.pmid","17369412"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1005"],["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","membrane biophysics"],["dc.title","Interaction of alamethicin pores in DMPC bilayers"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8235"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","8244"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Dubois, M."],["dc.contributor.author","Zemb, T"],["dc.date.accessioned","2017-09-07T11:44:16Z"],["dc.date.available","2017-09-07T11:44:16Z"],["dc.date.issued","2003"],["dc.description.abstract","We report an X-ray reflectivity study on highly charged lamellar phases of the surfactant didodecyldimethylammonium halides (DDA(+)X(-) where X- = Cl- or Br-). A few thousand bilayers are aligned on a flat solid surface with a mosaicity below 0.01degrees and are swollen under controlled osmotic pressure (Pi) from periodicities (d) of a few nanometers up to several tens of nanometers by means of direct immersion in the osmotic stressor reservoir. The high-pressure regime (small d) is obtained by water vapor of controlled relative humidity, while lower pressures (high d) are imposed by means of a novel osmotic stress technique. Accordingly, the solid supported sample is immersed in a high mass polyelectrolyte solution with the same sign and counterions than the membranes under study. Thus, water equilibrating time is reduced from weeks to minutes due to the absence of a semipermeable dialysis membrane. Measurements of the specular and nonspecular X-ray reflectivity are demonstrated to be possible through the osmotic reservoir even with a laboratory X-ray tube which greatly simplifies the establishment of the equation of state Pi(d). With the same setup, bilayer undulations and compressibility fluctuations can be studied by peak line shape analysis of high-resolution synchrotron data."],["dc.identifier.doi","10.1021/la034733j"],["dc.identifier.gro","3144058"],["dc.identifier.isi","000185690600019"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1640"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0743-7463"],["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","Highly oriented, charged multilamellar membranes osmotically stressed by a polyelectrolyte of the same sign"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","031706"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Physical Review E"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Constantin, Doru"],["dc.contributor.author","Brotons, Guillaume"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Freyssingeas, Eric"],["dc.contributor.author","Madsen, Anders"],["dc.date.accessioned","2017-09-07T11:52:37Z"],["dc.date.available","2017-09-07T11:52:37Z"],["dc.date.issued","2006"],["dc.description.abstract","Using x-ray photon correlation spectroscopy, we studied the layer fluctuations in the lamellar phase of an ionic lyotropic system. We measured the relaxation rate of in-plane (undulation) fluctuations as a function of the wave vector. Static and dynamic results obtained during the same experiment were combined to yield the values of both elastic constants of the lamellar phase (compression and bending moduli) as well as that of the sliding viscosity. The results are in very good agreement with dynamic light-scattering data, validating the use of the technique in ordered phases."],["dc.identifier.doi","10.1103/PhysRevE.74.031706"],["dc.identifier.gro","3143640"],["dc.identifier.isi","000240870100078"],["dc.identifier.pmid","17025653"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1176"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1539-3755"],["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","Dynamics of bulk fluctuations in a lamellar phase studied by coherent x-ray scattering"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","960"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Analytical and Bioanalytical Chemistry"],["dc.bibliographiccitation.lastpage","973"],["dc.bibliographiccitation.volume","379"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Brotons, Guillaume"],["dc.date.accessioned","2017-09-07T11:43:19Z"],["dc.date.available","2017-09-07T11:43:19Z"],["dc.date.issued","2004"],["dc.description.abstract","In this review article we discuss the thin film analytical techniques of interface sensitive X-ray and neutron scattering applied to aligned stacks of amphiphilic bilayers, in particular phospholipid membranes in the fluid La phase. We briefly discuss how the structure, composition, fluctuations and interactions in lipid or synthetic membranes can be studied by modern surface sensitive scattering techniques, using X-rays or neutrons as a probe. These techniques offer an in-situ approach to study lipid bilayer systems in different environments over length scales extending from micrometer to manometer, both with and without additional membrane-active molecules such as amphiphilic peptides or membrane proteins."],["dc.identifier.doi","10.1007/s00216-004-2696-9"],["dc.identifier.gro","3143960"],["dc.identifier.isi","000224054300008"],["dc.identifier.pmid","15338090"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1531"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1618-2650"],["dc.relation.issn","1618-2642"],["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","Biomolecular and amphiphilic films probed by surface sensitive X-ray and neutron scattering"],["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"]]