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.artnumber","072127"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","AIP Advances"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Reusch, Tobias"],["dc.contributor.author","Schuelein, Florian J. R."],["dc.contributor.author","Boemer, C."],["dc.contributor.author","Osterhoff, Markus"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Krenner, Hubert J."],["dc.contributor.author","Wixforth, Achim"],["dc.contributor.author","Salditt, Tim"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","We have carried out time resolved stroboscopic diffraction experiments on standing surface acoustic waves (SAWs) of Rayleigh type on a LiNbO3 substrate. A novel timing system has been developed and commissioned at the storage ring Petra III of Desy, allowing for phase locked stroboscopic diffraction experiments applicable to a broad range of timescales and experimental conditions. The combination of atomic structural resolution with temporal resolution on the picosecond time scale allows for the observation of the atomistic displacements for each time (or phase) point within the SAW period. A seamless transition between dynamical and kinematic scattering regimes as a function of the instantaneous surface amplitude induced by the standing SAW is observed. The interpretation and control of the experiment, in particular disentangling the diffraction effects (kinematic to dynamical diffraction regime) from possible non-linear surface effects is unambiguously enabled by the precise control of phase between the standing SAW and the synchrotron bunches. The example illustrates the great flexibility and universality of the presented timing system, opening up new opportunities for a broad range of time resolved experiments. (C) 2013 Author(s). All article content, except where otherwise noted, is licensed under a Creative Commons Attribution 3.0 Unported License."],["dc.identifier.doi","10.1063/1.4816801"],["dc.identifier.fs","600179"],["dc.identifier.gro","3142331"],["dc.identifier.isi","000322527000027"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10607"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7097"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2158-3226"],["dc.relation.orgunit","Fakultät für Physik"],["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.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Standing surface acoustic waves in LiNbO3 studied by time resolved X-ray diffraction at Petra III"],["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","417"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.lastpage","436"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Schneggenburger, Philipp Erik"],["dc.contributor.author","Beerlink, André"],["dc.contributor.author","Weinhausen, Britta"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2017-09-07T11:44:19Z"],["dc.date.available","2017-09-07T11:44:19Z"],["dc.date.issued","2011"],["dc.description.abstract","Studying membrane active peptides or protein fragments within the lipid bilayer environment is particularly challenging in the case of synthetically modified, labeled, artificial, or recently discovered native structures. For such samples the localization and orientation of the molecular species or probe within the lipid bilayer environment is the focus of research prior to an evaluation of their dynamic or mechanistic behavior. X-ray scattering is a powerful method to study peptide/lipid interactions in the fluid, fully hydrated state of a lipid bilayer. For one, the lipid response can be revealed by observing membrane thickening and thinning as well as packing in the membrane plane; at the same time, the distinct positions of peptide moieties within lipid membranes can be elucidated at resolutions of up to several angstroms by applying heavy-atom labeling techniques. In this study, we describe a generally applicable X-ray scattering approach that provides robust and quantitative information about peptide insertion and localization as well as peptide/lipid interaction within highly oriented, hydrated multilamellar membrane stacks. To this end, we have studied an artificial, designed beta-helical peptide motif in its homodimeric and hairpin variants adopting different states of oligomerization. These peptide lipid complexes were analyzed by grazing incidence diffraction (GID) to monitor changes in the lateral lipid packing and ordering. In addition, we have applied anomalous reflectivity using synchrotron radiation as well as in-house X-ray reflectivity in combination with iodine-labeling in order to determine the electron density distribution rho(z) along the membrane normal (z axis), and thereby reveal the hydrophobic mismatch situation as well as the position of certain amino acid side chains within the lipid bilayer. In the case of multiple labeling, the latter technique is not only applicable to demonstrate the peptide's reconstitution but also to generate evidence about the relative peptide orientation with respect to the lipid bilayer."],["dc.identifier.doi","10.1007/s00249-010-0645-4"],["dc.identifier.fs","589443"],["dc.identifier.gro","3142754"],["dc.identifier.isi","000289119700007"],["dc.identifier.pmid","21181143"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6600"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/193"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.publisher.place","New York"],["dc.relation.conference","455th Seminar on Biophysics of Membrane Active Peptides"],["dc.relation.eventlocation","Bad Honnef, GERMANY"],["dc.relation.ispartof","European Biophysics Journal"],["dc.relation.issn","0175-7571"],["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","Goescholar"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.gro","x-ray scattering"],["dc.subject.gro","membrane biophysics"],["dc.title","Peptide model helices in lipid membranes: insertion, positioning, and lipid response on aggregation studied by X-ray scattering"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]