Beerlink, André

[["dc.bibliographiccitation.artnumber","118102"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Physical Review Letters"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Reusch, Tobias"],["dc.contributor.author","Schuelein, Florian J. R."],["dc.contributor.author","Nicolas, Jan-David"],["dc.contributor.author","Osterhoff, Markus"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Krenner, Hubert J."],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Wixforth, Achim"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2020-11-05T15:05:24Z"],["dc.date.available","2020-11-05T15:05:24Z"],["dc.date.issued","2014"],["dc.description.abstract","We use standing surface acoustic waves to induce coherent phonons in model lipid multilayers deposited on a piezoelectric surface. Probing the structure by phase-controlled stroboscopic x-ray pulses we find that the internal lipid bilayer electron density profile oscillates in response to the externally driven motion of the lipid film. The structural response to the well-controlled motion is a strong indication that bilayer structure and membrane fluctuations are intrinsically coupled, even though these structural changes are averaged out in equilibrium and time integrating measurements. Here the effects are revealed by a timing scheme with temporal resolution on the picosecond scale in combination with the sub-nm spatial resolution, enabled by high brilliance synchrotron x-ray reflectivity."],["dc.identifier.doi","10.1103/PhysRevLett.113.118102"],["dc.identifier.gro","3142054"],["dc.identifier.isi","000345970800012"],["dc.identifier.pmid","25260008"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11552"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/68462"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-352.6"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1079-7114"],["dc.relation.issn","0031-9007"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0/"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Collective Lipid Bilayer Dynamics Excited by Surface Acoustic Waves"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1567"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","ChemPhysChem"],["dc.bibliographiccitation.lastpage","1576"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Worbs, Brigitte"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:46:52Z"],["dc.date.available","2017-09-07T11:46:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Structural parameters, such as conformation, orientation and penetration depth of membrane-bound peptides and proteins that may function as channels, pores or biocatalysts, are of persistent interest and have to be probed in the native fluid state of a membrane. X-ray scattering in combination with heavy-atom labeling is a powerful and highly appropriate method to reveal the position of a certain amino acid residue within a lipid bilayer with respect to the membrane normal axis up to a resolution of several Angstrom. Herein, we report the synthesis of a new iodine-labeled amino acid building block. This building block is intended for peptide incorporation to provide high intensities for electron density difference analysis of X-ray reflectivity data and improve the labeling potential for the lipid bilayer head-group and water region. The novel building block as well as the commercially available non-iodinated analogue, required for X-ray scattering, was implemented in a transmembrane peptide motif via manual solid-phase peptide synthesis (SPPS) following the fluorenylmethyloxycarbonyl (Fmoc)-strategy. The derived peptides were reconstituted in lipid vesicles as well as in highly aligned multilamellar lipid stacks and investigated via circular dichroism (CD) and X-ray reflectivity. Thereby, it has been revealed that the bulky iodine probe neither causes conformational change of the peptide structure nor lamellar disordering of the membrane complexes."],["dc.identifier.doi","10.1002/cphc.200900241"],["dc.identifier.gro","3143086"],["dc.identifier.isi","000267928100032"],["dc.identifier.pmid","19565579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/561"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB 803]"],["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","A Novel Heavy-Atom Label for Side-Specific Peptide Iodination: Synthesis, Membrane Incorporation and 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","2573"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The Journal of Physical Chemistry Letters"],["dc.bibliographiccitation.lastpage","2579"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Manor, Joshua"],["dc.contributor.author","Arbely, Eyal"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Akkawi, Mutaz"],["dc.contributor.author","Arkin, Isaiah T."],["dc.date.accessioned","2018-11-07T09:36:45Z"],["dc.date.available","2018-11-07T09:36:45Z"],["dc.date.issued","2014"],["dc.description.abstract","Solving structures of membrane proteins has always been a formidable challenge, yet even upon success, the results are normally obtained in a mimetic environment that can be substantially different from a biological membrane. Herein, we use noninvasive isotope-edited FTIR spectroscopy to derive a structural model for the SARS coronavirus E protein transmembrane domain in lipid bilayers. Molecular-dynamics-based structural refinement, incorporating the IR-derived orientational restraints points to the formation of a helical hairpin structure. Disulfide cross-linking and X-ray reflectivity depth profiling provide independent support of the results. The unusually short helical hairpin structure of the protein might explain its ability to deform bilayers and is reminiscent of other peptides with membrane disrupting fiinctionalities. Taken together, we show that isotope-edited FTIR is a powerful tool to analyze small membrane proteins in their native environment, enabling us to relate the unusual structure of the SAPS E protein to its function."],["dc.identifier.doi","10.1021/jz501055d"],["dc.identifier.isi","000340222200014"],["dc.identifier.pmid","26277945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32685"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation","SFB 755: Nanoscale Photonic Imaging"],["dc.relation.issn","1948-7185"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.title","Use of Isotope-Edited FTIR to Derive a Backbone Structure of a Transmembrane 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","337a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","338a"],["dc.bibliographiccitation.volume","100"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Mell, Michael"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2020-03-11T09:50:03Z"],["dc.date.available","2020-03-11T09:50:03Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1016/j.bpj.2010.12.2047"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63296"],["dc.language.iso","en"],["dc.relation.issn","0006-3495"],["dc.title","X-Ray Phase Contrast Imaging of Freestanding Lipid Model Membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","295"],["dc.bibliographiccitation.lastpage","296"],["dc.bibliographiccitation.volume","2007"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Boye, P."],["dc.contributor.author","Giewekemeyer, Klaus"],["dc.contributor.author","Gulden, Johannes"],["dc.contributor.author","Meents, Alke"],["dc.contributor.author","Neubauer, H."],["dc.contributor.author","Schropp, Andreas"],["dc.contributor.author","Stephan, S."],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Schroer, Christian G."],["dc.contributor.author","Vartaniants, I."],["dc.contributor.author","Weckert, E."],["dc.date.accessioned","2020-03-11T10:13:50Z"],["dc.date.available","2020-03-11T10:13:50Z"],["dc.date.issued","2007"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63298"],["dc.language.iso","en"],["dc.notes.preprint","yes"],["dc.relation.crisseries","Jahresbericht (Hamburger Synchrotronstrahlungslabor am Deutschen Elektronen-Synchrotron DESY)"],["dc.relation.eventend","2007"],["dc.relation.eventlocation","Hamburg"],["dc.relation.eventstart","2007"],["dc.relation.iserratumof","yes"],["dc.relation.ispartofseries","HASYLAB Jahresbericht;"],["dc.title","Coherent X-ray Diffraction Measurements at the cSAX beamline at SLS"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","203703"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Applied Physics Letters"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Mell, M."],["dc.contributor.author","Tolkiehn, M."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:46:47Z"],["dc.date.available","2017-09-07T11:46:47Z"],["dc.date.issued","2009"],["dc.description.abstract","We report hard x-ray phase contrast imaging of black lipid membranes, freely suspended over a micromachined aperture in an aqueous solution. Biomolecular and organic substances can thus be probed in hydrated environments by parallel beam propagation imaging, using coherent multi-kilo-electronvolt x-ray radiation. The width of the thinning film can be resolved from analysis of the intensity fringes in the Fresnel diffraction regime down to about 200 nm. The thinning process, in which solvent is expelled from the space in between two opposing monolayers, is monitored, and the domain walls between coexisting domains of swollen and thinned membrane patches are characterized."],["dc.identifier.doi","10.1063/1.3263946"],["dc.identifier.gro","3143024"],["dc.identifier.isi","000272052200077"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/493"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SFB755]; [ID10C]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0003-6951"],["dc.subject.gro","x-ray optics and imaging"],["dc.title","Hard x-ray phase contrast imaging of black lipid membranes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.seriesnr","1"],["dc.contributor.author","Beerlink, André"],["dc.date.accessioned","2018-05-03T10:48:01Z"],["dc.date.available","2018-05-03T10:48:01Z"],["dc.date.issued","2011"],["dc.description.abstract","Membranes fulfill many different functions inside a cell and have consequently been in the focus of biophysical studies for several decades. High resolution structure analysis of model membrane systems by x-ray reflectivity is typically performed using stabilizing solid supports, which have shown to strongly interact with the membranes and can severly affect the membrane`s functionality. To circumvent these restrictions free-standing lipid model membranes, also called Black Lipid Membranes (BLMs), have been used in this work towards a novel type of structural assay based on x-ray phase contrast imaging. Bulged lipid bilayers fully immersed in buffer solution have been visualized by a transmitted plane or spherical x-ray wave front in the Fresnel regime after free space propagation. The development of the experimental system and the image analysis enables a quantitative investigation of the membrane`s structural properties in a localized membrane patch. In future this technique can be used to study the structure of membranes and more generally ultrathin films in functional and physiological environments and under out-of-equilibrium conditions."],["dc.format.extent","III, 140"],["dc.identifier.doi","10.17875/gup2011-108"],["dc.identifier.isbn","978-3-941875-96-8"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6361"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14583"],["dc.identifier.urn","urn:nbn:de:gbv:7-isbn-978-3-941875-96-8-3"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","zu prüfen"],["dc.publisher","Universitätsverlag Göttingen"],["dc.publisher.place","Göttingen"],["dc.relation.crisseries","Göttingen Series in X-Ray Physics"],["dc.relation.ispartofseries","Göttingen Series in x-ray Physics; 01"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.access","openAccess"],["dc.rights.uri","https://creativecommons.org/licenses/by-nd/2.0"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","530"],["dc.title","Black lipid membranes studied by x-ray phase contrast imaging"],["dc.type","thesis"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4595"],["dc.bibliographiccitation.issue","17"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","4601"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Thutupalli, Shashi"],["dc.contributor.author","Mell, Michael"],["dc.contributor.author","Bartels, Matthias"],["dc.contributor.author","Cloetens, Peter"],["dc.contributor.author","Herminghaus, Stephan"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:51:49Z"],["dc.date.available","2017-09-07T11:51:49Z"],["dc.date.issued","2012"],["dc.description.abstract","We have used X-ray propagation imaging to visualize a less than 5 nm thick native lipid bilayer membrane freely suspended in aqueous solution. Contrast is formed by free space propagation of hard X-rays, with the membrane illuminated by a nano-focused, partially coherent synchrotron beam, at a controllable distance (defocus) behind the focal spot. Quantitative fitting of the magnified Fresnel fringes shows the transition from membranes swollen with solvent to the native bilayer, containing structural information at near-molecular resolution along the dimension perpendicular to the bilayer. We show first applications of this hybrid technique of propagation imaging and near-field diffraction to the investigation of ultra-thin organic films formed in micro-fluidic devices, namely the formation of a lipid bilayer by the adhesion of two constitutive monolayers."],["dc.identifier.doi","10.1039/c2sm00032f"],["dc.identifier.fs","585071"],["dc.identifier.gro","3146177"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10476"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3931"],["dc.language.iso","en"],["dc.notes","This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively."],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","1744-683X"],["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.subject.gro","x-ray imaging"],["dc.subject.gro","membrane biophysics"],["dc.title","X-Ray propagation imaging of a lipid bilayer in solution"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Physics in Medicine and Biology"],["dc.bibliographiccitation.volume","57"],["dc.contributor.author","Olendrowitz, Christian"],["dc.contributor.author","Bartels, Matthias"],["dc.contributor.author","Krenkel, Martin"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Mokso, R."],["dc.contributor.author","Sprung, Michael"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:48:27Z"],["dc.date.available","2017-09-07T11:48:27Z"],["dc.date.issued","2012"],["dc.description.abstract","We have analyzed the model organism Caenorhabditis elegans with the help of phase-contrast x-ray tomography. This work combines techniques from x-ray imaging studies of single biological cells by in-line holography with three-dimensional reconstruction and furthermore extends these studies to the multicellular level. To preserve the sub-cellular ultrastructure of the nematodes, we used the near-native sample preparation of high-pressure freezing as commonly used in the field of electron microscopy. For the presented samples, a standard, non-magnifying parallel-beam setting, as well as a magnifying, divergent-beam setting using nanofocusing optics is evaluated based on their tomographic reconstruction potential. In this paper, we address difficulties in sample preparation and issues of image processing. By experimental refinement and through optimized reconstruction procedures, we were able to perform x-ray imaging studies on a living specimen."],["dc.identifier.doi","10.1088/0031-9155/57/16/5309"],["dc.identifier.gro","3142478"],["dc.identifier.isi","000307112600017"],["dc.identifier.pmid","22853964"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8729"],["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","0031-9155"],["dc.relation.orgunit","Institut für Röntgenphysik"],["dc.relation.workinggroup","RG Salditt (Structure of Biomolecular Assemblies and X-Ray Physics)"],["dc.subject.gro","x-ray imaging"],["dc.subject.gro","biomedical tomography"],["dc.title","Phase-contrast x-ray imaging and tomography of the nematode Caenorhabditis elegans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","s74"],["dc.bibliographiccitation.issue","a1"],["dc.bibliographiccitation.journal","Acta Crystallographica. Section A, Foundations and Advances"],["dc.bibliographiccitation.lastpage","s74"],["dc.bibliographiccitation.volume","65"],["dc.contributor.author","Giewekemeyer, Klaus"],["dc.contributor.author","Kalbfleisch, Sebastian"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Kewish, Cameron M."],["dc.contributor.author","Thibault, Pierre"],["dc.contributor.author","Pfeiffer, Franz"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2020-03-11T09:54:42Z"],["dc.date.available","2020-03-11T09:54:42Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1107/S0108767309098560"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63297"],["dc.language.iso","en"],["dc.relation.issn","0108-7673"],["dc.title","Highly sensitive quantitative biological imaging by scanning X-ray diffraction microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]