Risselada, Herre Jelger

[["dc.bibliographiccitation.firstpage","10705"],["dc.bibliographiccitation.issue","45"],["dc.bibliographiccitation.journal","Soft Matter"],["dc.bibliographiccitation.lastpage","10718"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Smirnova, Yuliya G."],["dc.contributor.author","Aeffner, Sebastian"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Salditt, Tim"],["dc.contributor.author","Marrink, S. J."],["dc.contributor.author","Mueller, M."],["dc.contributor.author","Knecht, Volker"],["dc.date.accessioned","2017-09-07T11:48:19Z"],["dc.date.available","2017-09-07T11:48:19Z"],["dc.date.issued","2013"],["dc.description.abstract","Here we report studies on biologically important intermembrane repulsion forces using molecular dynamics (MD) simulations and experimental (osmotic stress) investigations of repulsion forces between 1-palmitoyl-2-oleyl-sn-glycero-3-phosphocholine bilayers. We show that the repulsion between tension-free membranes can be determined from MD simulations by either (i) simulating membrane stacks under different hydration conditions (unrestrained setup) and monitoring the change in the area per lipid upon dehydration or (ii) simulating two single punctured membranes immersed in a water reservoir and controlling the center-of-mass distance between the bilayers using an external potential (umbrella sampling setup). Despite the coarse-grained nature of the (MARTINI) model employed, the disjoining pressure profiles obtained from the simulations are in good agreement with our experiments. Remarkably, the two setups behave very differently in terms of membrane structure, as explained by considerations using elasticity theory, and the balance of interactions. In the unrestrained setup, dehydration decreases the area per lipid and lipid entropy. Dehydration in the umbrella sampling setup, in contrast, leads to an increase in area per lipid and lipid entropy. Hence, in the latter case, entropic effects from protrusion and zippering forces appear to be overcompensated by the entropy gain due to the disorder emerging from the expansion of the bilayers. The balance of interactions involves near cancellation of large opposing terms, for which also intramembrane and water-water interactions are important, and which appears to be largely a consequence, rather than the cause, of the intermembrane repulsion. Hence, care must be taken when drawing conclusions on the origin of intermembrane repulsion from thermodynamic analyses."],["dc.identifier.doi","10.1039/c3sm51771c"],["dc.identifier.fs","599527"],["dc.identifier.gro","3142410"],["dc.identifier.isi","000326456800006"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10828"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7974"],["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","WoS Import 2017-03-10 / Funder: VW-foundation; [SFB-803]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1744-6848"],["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","membrane biophysics"],["dc.title","Interbilayer repulsion forces between tension-free lipid bilayers from simulation"],["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","14500"],["dc.bibliographiccitation.issue","42"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","14508"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Fischer, Timo"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Vink, Richard L. C."],["dc.date.accessioned","2018-11-07T09:14:52Z"],["dc.date.available","2018-11-07T09:14:52Z"],["dc.date.issued","2012"],["dc.description.abstract","In experiments on model membranes, formation of large domains of different lipid composition is readily observed. However, no such phase separation is observed in the membranes of intact cells. Instead, small transient inhomogeneities called lipid rafts are expected in these systems. One of the numerous attempts to explain small domains refers to the coupling of the membrane to its surroundings, which leads to the immobilization of some of the membrane molecules. These immobilized molecules then act as static obstacles for the remaining mobile ones. We present detailed Molecular Dynamics simulations demonstrating that this can indeed account for small domains. This confirms previous Monte Carlo studies based on simplified models. Furthermore, by directly comparing domain structures obtained using Molecular Dynamics to Monte Carlo simulations of the Ising model, we demonstrate that domain formation in the presence of obstacles is remarkably insensitive to the details of the molecular interactions."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB 803]"],["dc.identifier.doi","10.1039/c2cp41417a"],["dc.identifier.isi","000309667100009"],["dc.identifier.pmid","22782576"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10226"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27530"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Royal Soc Chemistry"],["dc.relation.issn","1463-9076"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Membrane lateral structure: the influence of immobilized particles on domain size"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e38302"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.contributor.author","Marelli, Giovanni"],["dc.contributor.author","Fuhrmans, Marc"],["dc.contributor.author","Smirnova, Yuliya G."],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Marrink, Siewert Jan"],["dc.contributor.author","Mueller, Marcus"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","Our molecular simulations reveal that wild-type influenza fusion peptides are able to stabilize a highly fusogenic pre-fusion structure, i.e. a peptide bundle formed by four or more trans-membrane arranged fusion peptides. We rationalize that the lipid rim around such bundle has a non-vanishing rim energy (line-tension), which is essential to (i) stabilize the initial contact point between the fusing bilayers, i. e. the stalk, and (ii) drive its subsequent evolution. Such line-tension controlled fusion event does not proceed along the hypothesized standard stalk-hemifusion pathway. In modeled influenza fusion, single point mutations in the influenza fusion peptide either completely inhibit fusion (mutants G1V and W14A) or, intriguingly, specifically arrest fusion at a hemifusion state (mutant G1S). Our simulations demonstrate that, within a line-tension controlled fusion mechanism, these known point mutations either completely inhibit fusion by impairing the peptide's ability to stabilize the required peptide bundle (G1V and W14A) or stabilize a persistent bundle that leads to a kinetically trapped hemifusion state (G1S). In addition, our results further suggest that the recently discovered leaky fusion mutant G13A, which is known to facilitate a pronounced leakage of the target membrane prior to lipid mixing, reduces the membrane integrity by forming a 'super' bundle. Our simulations offer a new interpretation for a number of experimentally observed features of the fusion reaction mediated by the prototypical fusion protein, influenza hemagglutinin, and might bring new insights into mechanisms of other viral fusion reactions."],["dc.identifier.doi","10.1371/journal.pone.0038302"],["dc.identifier.fs","587227"],["dc.identifier.gro","3142512"],["dc.identifier.isi","000305826400002"],["dc.identifier.pmid","22761674"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7878"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8871"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1932-6203"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 2.5"],["dc.rights.uri","http://creativecommons.org/licenses/by/2.5/"],["dc.title","Line-Tension Controlled Mechanism for Influenza Fusion"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5984"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Milovanovic, Dragomir"],["dc.contributor.author","Honigmann, Alf"],["dc.contributor.author","Koike, Seiichi"],["dc.contributor.author","Göttfert, Fabian"],["dc.contributor.author","Pähler, Gesa"],["dc.contributor.author","Junius, Meike"],["dc.contributor.author","Müllar, Stefan"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Risselada, H. J."],["dc.contributor.author","Eggeling, Christian"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","van den Bogaart, Geert"],["dc.contributor.author","Jahn, Reinhard"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","The clustering of proteins and lipids in distinct microdomains is emerging as an important principle for the spatial patterning of biological membranes. Such domain formation can be the result of hydrophobic and ionic interactions with membrane lipids as well as of specific protein-protein interactions. Here using plasma membrane-resident SNARE proteins as model, we show that hydrophobic mismatch between the length of transmembrane domains (TMDs) and the thickness of the lipid membrane suffices to induce clustering of proteins. Even when the TMDs differ in length by only a single residue, hydrophobic mismatch can segregate structurally closely homologous membrane proteins in distinct membrane domains. Domain formation is further fine-tuned by interactions with polyanionic phosphoinositides and homo and heterotypic protein interactions. Our findings demonstrate that hydrophobic mismatch contributes to the structural organization of membranes."],["dc.identifier.doi","10.1038/ncomms6984"],["dc.identifier.fs","613597"],["dc.identifier.gro","3141986"],["dc.identifier.isi","000348812100002"],["dc.identifier.pmid","25635869"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13586"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3279"],["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","2041-1723"],["dc.rights.access","openAccess"],["dc.subject.mesh","Animals"],["dc.subject.mesh","Fluorescence Resonance Energy Transfer"],["dc.subject.mesh","Fluorescent Antibody Technique"],["dc.subject.mesh","Humans"],["dc.subject.mesh","Hydrophobic and Hydrophilic Interactions"],["dc.subject.mesh","Molecular Dynamics Simulation"],["dc.subject.mesh","Phosphatidylinositols"],["dc.subject.mesh","Protein Binding"],["dc.subject.mesh","Protein Structure, Tertiary"],["dc.subject.mesh","Rats"],["dc.subject.mesh","SNARE Proteins"],["dc.title","Hydrophobic mismatch sorts SNARE proteins into distinct membrane domains"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11242"],["dc.bibliographiccitation.issue","37"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","11246"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Gladytz, Anika"],["dc.contributor.author","Abel, Bernd"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.date.accessioned","2018-11-07T10:08:40Z"],["dc.date.available","2018-11-07T10:08:40Z"],["dc.date.issued","2016"],["dc.description.abstract","The question of how amyloid fibril formation is influenced by surfaces is crucial for a detailed understanding of the process invivo. We applied a combination of kinetic experiments and molecular dynamics simulations to elucidate how (model) surfaces influence fibril formation of the amyloid-forming sequences of prion protein SUP35 and human islet amyloid polypeptide. The kinetic data suggest that structural reorganization of the initial peptide corona around colloidal gold nanoparticles is the rate-limiting step. The molecular dynamics simulations reveal that partial physisorption to the surface results in the formation of aligned monolayers, which stimulate the formation of parallel, critical oligomers. The general mechanism implies that the competition between the underlying peptide-peptide and peptide-surface interactions must strike a balance to accelerate fibril formation."],["dc.identifier.doi","10.1002/anie.201605151"],["dc.identifier.isi","000383642300052"],["dc.identifier.pmid","27513605"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14027"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39507"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.publisher.place","Weinheim"],["dc.relation.conference","6th EuCheMS Chemistry Congress"],["dc.relation.eventlocation","Seville, SPAIN"],["dc.relation.issn","1521-3773"],["dc.relation.issn","1433-7851"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","Gold-Induced Fibril Growth: The Mechanism of Surface-Facilitated Amyloid Aggregation"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Physiology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","van Hilten, Niek"],["dc.contributor.author","Stroh, Kai Steffen"],["dc.contributor.author","Risselada, Herre Jelger"],["dc.date.accessioned","2020-12-10T18:44:38Z"],["dc.date.available","2020-12-10T18:44:38Z"],["dc.date.issued","2020"],["dc.description.abstract","Heterogeneities (e.g., membrane proteins and lipid domains) and deformations (e.g., highly curved membrane regions) in biological lipid membranes cause lipid packing defects that may trigger functional sorting of lipids and membrane-associated proteins. To study these phenomena in a controlled and efficient way within molecular simulations, we developed an external field protocol that artificially enhances packing defects in lipid membranes by enforcing local thinning of a flat membrane region. For varying lipid compositions, we observed strong thinning-induced depletion or enrichment, depending on the lipid's intrinsic shape and its effect on a membrane's elastic modulus. In particular, polyunsaturated and lysolipids are strongly attracted to regions high in packing defects, whereas phosphatidylethanolamine (PE) lipids and cholesterol are strongly repelled from it. Our results indicate that externally imposed changes in membrane thickness, area, and curvature are underpinned by shared membrane elastic principles. The observed sorting toward the thinner membrane region is in line with the sorting expected for a positively curved membrane region. Furthermore, we have demonstrated that the amphipathic lipid packing sensor (ALPS) protein motif, a known curvature and packing defect sensor, is effectively attracted to thinner membrane regions. By extracting the force that drives amphipathic molecules toward the thinner region, our thinning protocol can directly quantify and score the lipid packing sensing of different amphipathic molecules. In this way, our protocol paves the way toward high-throughput exploration of potential defect- and curvature-sensing motifs, making it a valuable addition to the molecular simulation toolbox."],["dc.identifier.doi","10.3389/fphys.2020.00250"],["dc.identifier.eissn","1664-042X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78537"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-042X"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Membrane Thinning Induces Sorting of Lipids and the Amphipathic Lipid Packing Sensor (ALPS) Protein Motif"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","343001"],["dc.bibliographiccitation.issue","34"],["dc.bibliographiccitation.journal","Journal of Physics. D, Applied Physics"],["dc.bibliographiccitation.volume","51"],["dc.contributor.affiliation","Bassereau, Patricia;"],["dc.contributor.affiliation","Jin, Rui;"],["dc.contributor.affiliation","Baumgart, Tobias;"],["dc.contributor.affiliation","Deserno, Markus;"],["dc.contributor.affiliation","Dimova, Rumiana;"],["dc.contributor.affiliation","Frolov, Vadim A;"],["dc.contributor.affiliation","Bashkirov, Pavel V;"],["dc.contributor.affiliation","Grubmüller, Helmut;"],["dc.contributor.affiliation","Jahn, Reinhard;"],["dc.contributor.affiliation","Risselada, H Jelger;"],["dc.contributor.affiliation","Johannes, Ludger;"],["dc.contributor.affiliation","Kozlov, Michael M;"],["dc.contributor.affiliation","Lipowsky, Reinhard;"],["dc.contributor.affiliation","Pucadyil, Thomas J;"],["dc.contributor.affiliation","Zeno, Wade F;"],["dc.contributor.affiliation","Stachowiak, Jeanne C;"],["dc.contributor.affiliation","Stamou, Dimitrios;"],["dc.contributor.affiliation","Breuer, Artù;"],["dc.contributor.affiliation","Lauritsen, Line;"],["dc.contributor.affiliation","Simon, Camille;"],["dc.contributor.affiliation","Sykes, Cécile;"],["dc.contributor.affiliation","Voth, Gregory A;"],["dc.contributor.affiliation","Weikl, Thomas R;"],["dc.contributor.author","Bassereau, Patricia"],["dc.contributor.author","Jin, Rui"],["dc.contributor.author","Baumgart, Tobias"],["dc.contributor.author","Deserno, Markus"],["dc.contributor.author","Dimova, Rumiana"],["dc.contributor.author","Frolov, Vadim A"],["dc.contributor.author","Bashkirov, Pavel V"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Jahn, Reinhard"],["dc.contributor.author","Risselada, H. Jelger"],["dc.contributor.author","Johannes, Ludger"],["dc.contributor.author","Kozlov, Michael M."],["dc.contributor.author","Lipowsky, Reinhard"],["dc.contributor.author","Pucadyil, Thomas J."],["dc.contributor.author","Zeno, Wade F."],["dc.contributor.author","Stachowiak, Jeanne C."],["dc.contributor.author","Stamou, Dimitrios"],["dc.contributor.author","Breuer, Artù"],["dc.contributor.author","Lauritsen, Line"],["dc.contributor.author","Simon, Camille"],["dc.contributor.author","Sykes, Cécile"],["dc.contributor.author","Voth, Gregory A."],["dc.contributor.author","Weikl, Thomas R."],["dc.date.accessioned","2020-12-10T18:15:41Z"],["dc.date.available","2020-12-10T18:15:41Z"],["dc.date.issued","2018"],["dc.date.updated","2022-02-09T13:18:50Z"],["dc.description.abstract","Abstract The importance of curvature as a structural feature of biological membranes has been recognized for many years and has fascinated scientists from a wide range of different backgrounds. On the one hand, changes in membrane morphology are involved in a plethora of phenomena involving the plasma membrane of eukaryotic cells, including endo- and exocytosis, phagocytosis and filopodia formation. On the other hand, a multitude of intracellular processes at the level of organelles rely on generation, modulation, and maintenance of membrane curvature to maintain the organelle shape and functionality. The contribution of biophysicists and biologists is essential for shedding light on the mechanistic understanding and quantification of these processes. Given the vast complexity of phenomena and mechanisms involved in the coupling between membrane shape and function, it is not always clear in what direction to advance to eventually arrive at an exhaustive understanding of this important research area. The 2018 Biomembrane Curvature and Remodeling Roadmap of Journal of Physics D: Applied Physics addresses this need for clarity and is intended to provide guidance both for students who have just entered the field as well as established scientists who would like to improve their orientation within this fascinating area."],["dc.identifier.doi","10.1088/1361-6463/aacb98"],["dc.identifier.eissn","1361-6463"],["dc.identifier.issn","0022-3727"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74924"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","IOP Publishing"],["dc.rights.uri","http://creativecommons.org/licenses/by/3.0/"],["dc.title","The 2018 biomembrane curvature and remodeling roadmap"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Biosciences"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Zoni, Valeria"],["dc.contributor.author","Nieto, Vincent"],["dc.contributor.author","Endter, Laura J."],["dc.contributor.author","Risselada, Herre J."],["dc.contributor.author","Monticelli, Luca"],["dc.contributor.author","Vanni, Stefano"],["dc.date.accessioned","2020-12-10T18:44:29Z"],["dc.date.available","2020-12-10T18:44:29Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.3389/fmolb.2019.00124"],["dc.identifier.eissn","2296-889X"],["dc.identifier.pmid","31799255"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78472"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","2296-889X"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","To Bud or Not to Bud: A Perspective on Molecular Simulations of Lipid Droplet Budding"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]