Ghosh, Sajal Kumar

[["dc.bibliographiccitation.firstpage","2633"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","2640"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Ghosh, Sajal Kumar"],["dc.contributor.author","Aeffner, Sebastian"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:43:23Z"],["dc.date.available","2017-09-07T11:43:23Z"],["dc.date.issued","2011"],["dc.description.abstract","Phosphatidylinositol 4,5-bis-phosphate (PIP2) is an important lipid in regulation of several cellular processes, particularly membrane fusion. We use X-ray diffraction from solid-supported multilamellar 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC)/PIP2 samples to study changes in bilayer structure and the lyotropic phase behavior induced by physiologically relevant concentrations of PIP2. Electron-density profiles reconstructed from X-ray reflectivity measurements indicate that PIP2 strongly affects structural parameters such as lipid head-group width, bilayer thickness, and lamellar repeat spacing of DOPC bilayer stacks. In addition, at lower degrees of hydration, a few molar per cent of PIP2 facilitates stalk-phase formation and also leads to formation of a hexagonal phase, which is not observed in pure DOPC. These results indicate that the role of PIP2 in membrane fusion could be, in part, due to its effect on the properties of the lipid bilayer matrix. Furthermore, coexistence of two lamellar phases with different lattice constants is observed in single-component PIP2 samples."],["dc.identifier.doi","10.1002/cphc.201100154"],["dc.identifier.gro","3142652"],["dc.identifier.isi","000295252900021"],["dc.identifier.pmid","21826776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/79"],["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","1439-4235"],["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","Effect of PIP2 on Bilayer Structure and Phase Behavior of DOPC: An X-ray Scattering Study"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","012015"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Physics: Conference Series"],["dc.bibliographiccitation.volume","247"],["dc.contributor.affiliation","S Castorph, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.affiliation","L Arleth, ; 2Biophysics, Faculty of Life Sciences, University of Copenhagen, Frederiksberg, DK"],["dc.contributor.affiliation","M Sztucki, ; 3European Synchrotron Radiation Facility, Grenoble, F"],["dc.contributor.affiliation","U Vainio, ; 4Hamburger Synchrotronstrahlungslabor at Deutsches Elektronen-Synchrotron, Hamburg, D"],["dc.contributor.affiliation","S K Ghosh, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.affiliation","M Holt, ; 5Max Planck Institut für Biophysikalische Chemie, Department of Neurobiology, Göttingen, D"],["dc.contributor.affiliation","R Jahn, ; 5Max Planck Institut für Biophysikalische Chemie, Department of Neurobiology, Göttingen, D"],["dc.contributor.affiliation","T Salditt, ; 1Institut für Röntgenphysik, Georg-August-Universität Göttingen, Göttingen, D"],["dc.contributor.author","Castorph, Simon"],["dc.contributor.author","Arleth, Lise"],["dc.contributor.author","Sztucki, Michael"],["dc.contributor.author","Vainio, Ulla"],["dc.contributor.author","Ghosh, S. K."],["dc.contributor.author","Holt, M."],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:54:07Z"],["dc.date.available","2017-09-07T11:54:07Z"],["dc.date.issued","2010"],["dc.date.updated","2022-02-18T08:56:36Z"],["dc.description.abstract","We discuss different spherically symmetric and anisotropic form factor models and test them against high resolution synchrotron based small-angle x-ray scattering (SAXS) data from synaptic vesicles (SVs), isolated from rat brain. Anisotropy of the model form factors is found to be a key ingredient for the description of the native synaptic vesicle structure. We describe changes in structural parameters due to protease digestion of SVs, and present SAXS data of SVs recorded under different pH conditions."],["dc.identifier.doi","10.1088/1742-6596/247/1/012015"],["dc.identifier.fs","581310"],["dc.identifier.gro","3145120"],["dc.identifier.issn","1742-6596"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7197"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2821"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.relation.issn","1742-6596"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.orgunit","Fakultät für Physik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights.uri","https://publishingsupport.iopscience.iop.org/open_access/"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","neuro biophysics"],["dc.title","Synaptic Vesicles Studied by SAXS: Derivation and Validation of a Model Form Factor"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]