Komorowski, Karlo

[["dc.bibliographiccitation.firstpage","43"],["dc.bibliographiccitation.lastpage","86"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Frank, Kilian"],["dc.contributor.editor","Nieh, Mu-Ping"],["dc.contributor.editor","Heberle, Frederick A."],["dc.contributor.editor","Katsaras, John"],["dc.date.accessioned","2020-03-03T08:14:53Z"],["dc.date.available","2020-03-03T08:14:53Z"],["dc.date.issued","2019"],["dc.description.abstract","In this chapter, we describe X-ray diffraction analysis of lipid model membranes, including fundamentals of experiment and analysis. We start with solid-supported single bilayers and monolayers, then discuss solid-supported multilamellar stacks, and finally vesicles in solution. For oriented membranes, we discuss specular and nonspecular reflectivity, as well as grazing incidence diffraction, and for vesicles we discuss small-angle X-ray scattering. In each case, illustrative examples of current applications are given. The chapter closes with an outlook on free electron laser sources and new opportunities for research on lipid model membranes and biomembranes."],["dc.identifier.doi","10.1515/9783110544657-002"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63066"],["dc.language.iso","en"],["dc.publisher","De Gruyter"],["dc.publisher.place","Berlin, Boston"],["dc.relation.eisbn","978-3-11-054465-7"],["dc.relation.ispartof","Characterization of Biological Membranes: Structure and Dynamics"],["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","X-ray structure analysis of lipid membrane systems: solid-supported bilayers, bilayer stacks, and vesicles"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","566"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Biomembranes"],["dc.bibliographiccitation.lastpage","578"],["dc.bibliographiccitation.volume","1860"],["dc.contributor.author","Xu, Yihui"],["dc.contributor.author","Kuhlmann, Jan"],["dc.contributor.author","Brennich, Martha"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2018-01-17T13:00:13Z"],["dc.date.available","2018-01-17T13:00:13Z"],["dc.date.issued","2018"],["dc.description.abstract","SNAREs are known as an important family of proteins mediating vesicle fusion. For various biophysical studies, they have been reconstituted into supported single bilayers via proteoliposome adsorption and rupture. In this study we extended this method to the reconstitution of SNAREs into supported multilamellar lipid membranes, i.e. oriented multibilayer stacks, as an ideal model system for X-ray structure analysis (X-ray reflectivity and diffraction). The reconstitution was implemented through a pathway of proteomicelle, proteoliposome and multibilayer. To monitor the structural evolution in each step, we used small-angle X-ray scattering for the proteomicelles and proteoliposomes, followed by X-ray reflectivity and grazing-incidence small-angle scattering for the multibilayers. Results show that SNAREs can be successfully reconstituted into supported multibilayers, with high enough orientational alignment for the application of surface sensitive X-ray characterizations. Based on this protocol, we then investigated the effect of SNAREs on the structure and phase diagram of the lipid membranes. Beyond this application, this reconstitution protocol could also be useful for X-ray analysis of many further membrane proteins."],["dc.identifier.doi","10.1016/j.bbamem.2017.10.023"],["dc.identifier.pmid","29106973"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11697"],["dc.language.iso","en"],["dc.notes.status","final"],["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","Reconstitution of SNARE proteins into solid-supported lipid bilayer stacks and X-ray structure analysis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","465"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","482"],["dc.bibliographiccitation.volume","51"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Preobraschenski, Julia"],["dc.contributor.author","Ganzella, Marcelo"],["dc.contributor.author","Alfken, Jette"],["dc.contributor.author","Neuhaus, Charlotte"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2022-09-01T09:51:27Z"],["dc.date.available","2022-09-01T09:51:27Z"],["dc.date.issued","2022-07-29"],["dc.description.abstract","The size, polydispersity, and electron density profile of synaptic vesicles (SVs) can be studied by small-angle X-ray scattering (SAXS), i.e. by X-ray diffraction from purified SV suspensions in solution. Here we show that size and shape transformations, as they appear in the functional context of these important synaptic organelles, can also be monitored by SAXS. In particular, we have investigated the active uptake of neurotransmitters, and find a mean vesicle radius increase of about 12% after the uptake of glutamate, which indicates an unusually large extensibility of the vesicle surface, likely to be accompanied by conformational changes of membrane proteins and rearrangements of the bilayer. Changes in the electron density profile (EDP) give first indications for such a rearrangement. Details of the protein structure are screened, however, by SVs polydispersity. To overcome the limitations of large ensemble averages and heterogeneous structures, we therefore propose serial X-ray diffraction by single free electron laser pulses. Using simulated data for realistic parameters, we show that this is in principle feasible, and that even spatial distances between vesicle proteins could be assessed by this approach."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Georg-August-Universität Göttingen 501100003385"],["dc.identifier.doi","10.1007/s00249-022-01609-w"],["dc.identifier.pii","1609"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113969"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1432-1017"],["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.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.gro","Synaptic vesicle"],["dc.subject.gro","Small angle X-ray scattering"],["dc.subject.gro","Neurotransmitter uptake"],["dc.subject.gro","Synchrotron and free electron laser techniques"],["dc.title","Neurotransmitter uptake of synaptic vesicles studied by X-ray diffraction"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","265"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.lastpage","278"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Scheu, Max"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Shen, Chen"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2022-06-08T07:59:20Z"],["dc.date.available","2022-06-08T07:59:20Z"],["dc.date.issued","2021"],["dc.description.abstract","In this work, we present evidence for the formation of transient stalks in aligned multilamellar stacks of lipid membranes. Just above the phase transition from the fluid ( 1029320L_\\alpha1029320 L α ) lamellar phase to the rhombohedral phase (R), where lipid stalks crystallize on a super-lattice within the lipid bilayer stack, we observe a characteristic scattering pattern, which can be attributed to a correlated fluid of transient stalks. Excess (off-axis) diffuse scattering with a broad modulation around the position which later transforms to a sharp peak of the rhombohedral lattice, gives evidence for the stalk fluid forming as a pre-critical effect, reminiscent of critical phenomena in the vicinity of second-order phase transitions. Using high-resolution off-specular X-ray scattering and lineshape analysis we show that this pre-critical regime is accompanied by an anomalous elasticity behavior of the membrane stack, in particular an increase in inter-bilayer compressibility, i.e., a decrease in the compression modulus."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","Projekt DEAL"],["dc.identifier.doi","10.1007/s00249-020-01493-2"],["dc.identifier.pii","1493"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/110713"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.relation.eissn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","A stalk fluid forming above the transition from the lamellar to the rhombohedral phase of lipid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","82a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Nehls, Christian"],["dc.contributor.author","Haas, Albert"],["dc.contributor.author","Komorowski, Karlo"],["dc.contributor.author","Gutsmann, Thomas"],["dc.date.accessioned","2020-03-03T08:19:03Z"],["dc.date.available","2020-03-03T08:19:03Z"],["dc.date.issued","2016"],["dc.description.abstract","The intracellular pathogen R. equi manages to survive the phagosome maturation by arresting phagosomes in a prephagolysosomal state. The rhodococcal virulence-associated protein A (VapA) contributes to this process [1]. We propose a pore forming activity for VapA.Based on experiments with model membranes mimicking the phagosome membrane we suggest a five-step mode of action for VapA. Biosensor experiments indicated a binding of VapA to the bilayers (1) being accompanied by an increase of membrane rigidity. In contrast to common pore-forming molecules only a weak intercalation dependent on the lateral membrane pressure occured (2). AFM analysis revealed a strong aggregation of VapA on cholesterol-poor lipid domains (3). This induced a reorganization of the domain structure of the bilayer. Defined and undefined lesions increasing the permeability of the reconstituted membranes (4) and finally the induction of membrane disintegration by VapA (5) were observed using electrophysiological measurements on freestanding membranes and a fluorescence based nanopore dye release assay.We assume two different interaction states for VapA defined by different protein orientation which depend on lipid package, lipid composition and pH value. The potential relevance of these observations for understanding of R. equi virulence will be discussed.References[1] von Bargen, C. and Haas, A., 2009, FEMS Microbiol Rev 33: 870-891."],["dc.identifier.doi","10.1016/j.bpj.2015.11.501"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63068"],["dc.language.iso","en"],["dc.relation.issn","0006-3495"],["dc.title","Investigation of the Mode of Action of the Protein VapA of Rhodococcus Equi on Phagosome Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dspace.entity.type","Publication"]]