Beerlink, André

[["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.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"]]

[["dc.bibliographiccitation.firstpage","4952"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Langmuir"],["dc.bibliographiccitation.lastpage","4958"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Wilbrandt, P. -J."],["dc.contributor.author","Ziegler, E."],["dc.contributor.author","Carbone, D."],["dc.contributor.author","Metzger, T. H."],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:48:43Z"],["dc.date.available","2017-09-07T11:48:43Z"],["dc.date.issued","2008"],["dc.description.abstract","Silicon and Teflon substrates have been structured by wet etching and a focused ion beam (FIB) to obtain very defined, clean apertures. Planar, free-standing lipid membranes (black lipid membranes (BLM)) with enhanced long-term stability have been prepared on these apertures by the methods of Montal and Muller(1,2) as well as Miller and Rudin.(3) The stability and geometric control enables the use of X-ray analysis of free-standing single bilayers. With the presented setup, simultaneous structural and electrophysiological measurements will become feasible."],["dc.identifier.doi","10.1021/la703704x"],["dc.identifier.gro","3143298"],["dc.identifier.isi","000255432000079"],["dc.identifier.pmid","18370435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/797"],["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","neuro biophysics"],["dc.title","X-ray structure analysis of free-standing lipid membranes facilitated by micromachined apertures"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Mell, Michael"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2018-11-07T08:53:37Z"],["dc.date.available","2018-11-07T08:53:37Z"],["dc.date.issued","2011"],["dc.identifier.isi","000293637300537"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22461"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.eventlocation","Budapest, HUNGARY"],["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","membrane biophysics"],["dc.title","Hard X-ray phase contrast imaging of black lipid membranes"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]