Bennati, Marina

[["dc.bibliographiccitation.journal","Journal of Peptide Science"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Muellar, S. M."],["dc.contributor.author","Schneggenburger, Philipp E."],["dc.contributor.author","Sicoli, Giuseppe"],["dc.contributor.author","Steinem, Claudia"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T08:39:53Z"],["dc.date.available","2018-11-07T08:39:53Z"],["dc.date.issued","2010"],["dc.format.extent","31"],["dc.identifier.isi","000281610800031"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19109"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-Blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1075-2617"],["dc.title","Synthesis of Artificial Membrane Peptides: Recognition, Assembly and Structural Studies at the Membrane/Water Interface"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","9743"],["dc.bibliographiccitation.issue","41"],["dc.bibliographiccitation.journal","Angewandte Chemie International Edition"],["dc.bibliographiccitation.lastpage","9746"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Stoller, Sven"],["dc.contributor.author","Sicoli, Giuseppe"],["dc.contributor.author","Baranova, Tatiana Y."],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T09:00:40Z"],["dc.date.available","2018-11-07T09:00:40Z"],["dc.date.issued","2011"],["dc.description.sponsorship","Deutsche Forschungs-gemeinschaft DFG [SFB 803]"],["dc.identifier.doi","10.1002/anie.201103315"],["dc.identifier.isi","000296205000048"],["dc.identifier.pmid","21898726"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24229"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1433-7851"],["dc.title","TOPP: A Novel Nitroxide-Labeled Amino Acid for EPR Distance Measurements"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3433"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Physical Chemistry Chemical Physics"],["dc.bibliographiccitation.lastpage","3437"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Tkach, Igor"],["dc.contributor.author","Pornsuwan, Soraya"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Wachowius, Falk"],["dc.contributor.author","Sigurdsson, Snorri Th."],["dc.contributor.author","Baranova, Tatiana Y."],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Sicoli, Giuseppe"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2018-11-07T09:30:21Z"],["dc.date.available","2018-11-07T09:30:21Z"],["dc.date.issued","2013"],["dc.description.abstract","Pulsed electron-electron double resonance (PELDOR, also known as DEER) has become a method of choice to measure distances in biomolecules. In this work we show how the performance of the method can be improved at high EPR frequencies (94 GHz) using variable dual frequency irradiation in a dual mode cavity in order to obtain enhanced resolution toward orientation selection. Dipolar evolution traces of a representative RNA duplex and an alpha-helical peptide were analysed in terms of possible bi-radical structures by considering the inherent ambiguity of symmetry-related solutions."],["dc.identifier.doi","10.1039/c3cp44415e"],["dc.identifier.isi","000314846600006"],["dc.identifier.pmid","23381580"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10192"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31286"],["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","Orientation selection in distance measurements between nitroxide spin labels at 94 GHz EPR with variable dual frequency irradiation"],["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.firstpage","2345"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","2348"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Halbmair, Karin"],["dc.contributor.author","Wegner, Janine"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2018-08-16T12:55:22Z"],["dc.date.available","2018-08-16T12:55:22Z"],["dc.date.issued","2016"],["dc.description.abstract","We present the performance of nanometer-range pulse electron paramagnetic resonance distance measurements (pulsed electron-electron double resonance/double electron-electron resonance, PELDOR/DEER) on a transmembrane WALP24 peptide labeled with the semirigid unnatural amino acid 4-(3,3,5,5-tetra-methyl-2,6-dioxo-4-oxylpiperazin-1-yl)-l-phenylglycine (TOPP). Distances reported by the TOPP label are compared to the ones reported by the more standard MTSSL spin label, commonly employed in protein studies. Using high-power pulse electron paramagnetic resonance spectroscopy at Q-band frequencies (34 GHz), we show that in contrast to MTSSL, our label reports one-peak, sharp (Δr ≤ 0.4 nm) intramolecular distances. Orientational selectivity is not observed. When spin-labeled WALP24 was inserted in two representative lipid bilayers with different bilayer thickness, i.e., DMPC and POPC, the intramolecular distance reported by TOPP did not change with the bilayer environment. In contrast, the distance measured with MTSSL was strongly affected by the hydrophobic thickness of the lipid. The results demonstrate that the TOPP label is well suited to study the intrinsic structure of peptides immersed in lipids."],["dc.identifier.doi","10.1016/j.bpj.2016.10.022"],["dc.identifier.pmid","27836102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15353"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1542-0086"],["dc.relation.eissn","0006-3495"],["dc.title","Pulse EPR Measurements of Intramolecular Distances in a TOPP-Labeled Transmembrane Peptide in Lipids"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2203-2207"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Chemistry: a European Journal"],["dc.bibliographiccitation.lastpage","2207"],["dc.bibliographiccitation.volume","25"],["dc.contributor.author","Wegner, Janine"],["dc.contributor.author","Valora, Gabriele"],["dc.contributor.author","Halbmair, Karin"],["dc.contributor.author","Kehl, Annemarie"],["dc.contributor.author","Worbs, Brigitte"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2020-11-23T13:55:26Z"],["dc.date.available","2020-11-23T13:55:26Z"],["dc.date.issued","2019-02-11"],["dc.description.abstract","β-Peptides are an interesting new class of transmembrane model peptides based on their conformationally stable and well-defined secondary structures. Herein, we present the synthesis of the paramagnetic β-amino acid β3 -hTOPP (4-(3,3,5,5-tetramethyl-2,6-dioxo-4-oxylpiperazin-1-yl)-d-β3 -homophenylglycine) that enables investigations of β-peptides by EPR spectroscopy. This amino acid adds to the, to date, sparse number of β-peptide spin labels. Its performance was evaluated by investigating the helical turn of a 314 -helical transmembrane model β-peptide. Nanometer distances between two incorporated β3 -hTOPP labels in different environments were measured by using pulsed electron/electron double resonance (PELDOR/DEER) spectroscopy. Due to the semi-rigid conformational design, the label delivers reliable distances and sharp (one-peak) distance distributions even in the lipid bilayer. The results indicate that the investigated β-peptide folds into a 3.2514 helix and maintains this conformation in the lipid bilayer."],["dc.identifier.doi","10.1002/chem.201805880"],["dc.identifier.pmid","30500095"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/69025"],["dc.language.iso","en"],["dc.relation.eissn","1521-3765"],["dc.relation.issn","0947-6539"],["dc.title","Semi-Rigid Nitroxide Spin Label for Long-Range EPR Distance Measurements of Lipid Bilayer Embedded β-Peptides"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Biophysics Journal"],["dc.contributor.author","Tkach, Igor"],["dc.contributor.author","Diederichsen, Ulf"],["dc.contributor.author","Bennati, Marina"],["dc.date.accessioned","2021-04-14T08:29:17Z"],["dc.date.available","2021-04-14T08:29:17Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1007/s00249-021-01508-6"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82858"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1432-1017"],["dc.relation.issn","0175-7571"],["dc.title","Studies of transmembrane peptides by pulse dipolar spectroscopy with semi-rigid TOPP spin labels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Peptide Science"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Wegner, J."],["dc.contributor.author","Halbmair, Karin"],["dc.contributor.author","Bennati, Marina"],["dc.contributor.author","Diederichsen, Ulf"],["dc.date.accessioned","2018-11-07T10:08:43Z"],["dc.date.available","2018-11-07T10:08:43Z"],["dc.date.issued","2016"],["dc.format.extent","S76"],["dc.identifier.isi","000398216100134"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39520"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley"],["dc.publisher.place","Hoboken"],["dc.relation.issn","1099-1387"],["dc.relation.issn","1075-2617"],["dc.title","TOPP: A Rigid Spin Label for the Determination of Distances in A- and B-Transmembrane Peptides by EPR"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]