Seidel, Karsten

[["dc.bibliographiccitation.firstpage","4369"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","4376"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Seidel, Karsten"],["dc.contributor.author","Andronesi, Ovidiu C."],["dc.contributor.author","Krebs, Joachim"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Young, Howard S."],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Baldus, Marc"],["dc.date.accessioned","2017-09-07T11:48:45Z"],["dc.date.available","2017-09-07T11:48:45Z"],["dc.date.issued","2008"],["dc.description.abstract","Phospholamban (PLN) regulates cardiac contractility by modulation of sarco(endo)plasmic reticulum calcium ATPase (SERCA) activity. While PLN and SERCAla, an isoform from skeletal muscle, have been structurally characterized in great detail, direct information about the conformation of PLN in complex with SERCA has been limited. We used solid-state NMR (ssNMR) spectroscopy to deduce structural properties of both the A(36)F(41)A(46) mutant (AFA-PLN) and wild-type PLN (WT-PLN) when bound to SERCA I a after reconstitution in a functional lipid bilayer environment. Chemical-shift assignments in all domains of AFA-PLN provide direct evidence for the presence of two terminal a helices connected by a linker region of reduced structural order that differs from previous findings on free PLN. ssNMR experiments on WT-PLN show no significant difference in binding compared to AFA-PLN and do not support the coexistence of a significantly populated dynamic state of PLN after formation of the PLN/ SERCA complex. A combination of our spectroscopic data with biophysical and biochemical data using flexible protein-protein docking simulations provides a structural basis for understanding the interaction between PLN and SERCAla."],["dc.identifier.doi","10.1021/bi7024194"],["dc.identifier.gro","3143315"],["dc.identifier.isi","000254818100003"],["dc.identifier.pmid","18355039"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/816"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Structural characterization of Ca2+-ATPase-bound phospholarnban in lipid bilayers by solid-state nuclear magnetic resonance (NMR) Spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5922"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","Journal of the American Chemical Society"],["dc.bibliographiccitation.lastpage","5928"],["dc.bibliographiccitation.volume","130"],["dc.contributor.author","Andronesi, Ovidiu C."],["dc.contributor.author","von Bergen, Martin"],["dc.contributor.author","Biernat, Jacek"],["dc.contributor.author","Seidel, Karsten"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Mandelkow, Eckhard"],["dc.contributor.author","Baldus, Marc"],["dc.date.accessioned","2017-09-07T11:48:44Z"],["dc.date.available","2017-09-07T11:48:44Z"],["dc.date.issued","2008"],["dc.description.abstract","The polymerization of the microtubule-associated protein tau into paired helical filaments (PHFs) represents one of the hallmarks of Alzheimer's disease. We employed solid-state nuclear magnetic resonance (NMR) to investigate the structure and dynamics of PHFs formed in vitro by the three-repeat-domain (K19) of protein tau, representing the core of Alzheimer PHFs. While N and C termini of tau monomers in PHFs are highly dynamic and solvent-exposed, the rigid segment consists of three major P-strands. Combination of through-bond and through-space ssNMR transfer methods with water-edited (N-15, C-13) and (C-13, C-13) correlation experiments suggests the existence of a fibril core that is largely built by repeat unit R3, flanked by surface-exposed units R1 and R4. Solid-state NMR, circular dichroism, and the fibrillization behavior of a K19 mutant furthermore indicate that electrostatic interactions play a central role in stabilizing the K19 PHFs."],["dc.identifier.doi","10.1021/ja7100517"],["dc.identifier.gro","3143297"],["dc.identifier.isi","000255629400031"],["dc.identifier.pmid","18386894"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/796"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0002-7863"],["dc.title","Characterization of Alzheimer's-like paired helical filaments from the core domain of tau protein using solid-state NMR spectroscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]