title: Challenge of large-scale motion for residual dipolar coupling based analysis of configuration: the case of fibrosterol sulfate A.
abstract: Fibrosterol sulfate A is a polysulfated bis-steroid with an atypical side chain. Due to the flexibility of the linker, large-scale motions that change dramatically the shape of the entire molecule are expected. Such motions pose major challenges to the structure elucidation and the correct determination of configuration. In this study, we will describe the determination of the relative configuration of fibrosterol sulfate A through a residual dipolar coupling based multiple alignment tensor analysis complemented by molecular dynamics. For completeness, we applied also the single tensor approach which is unreliable due to the large-scale motions and compare the results.
authors.affiliation: Department of NMR Based Structural Biology, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Han
authors.initials: H
authors.lastname: Sun
authors.forename: Uwe M
authors.initials: UM
authors.lastname: Reinscheid
authors.forename: Emily L
authors.initials: EL
authors.lastname: Whitson
authors.forename: Edward J
authors.initials: EJ
authors.lastname: d'Auvergne
authors.forename: Chris M
authors.initials: CM
authors.lastname: Ireland
authors.forename: Armando
authors.initials: A
authors.lastname: Navarro-Vázquez
authors.forename: Christian
authors.initials: C
authors.lastname: Griesinger
mesh_terms: D009682:Magnetic Resonance Spectroscopy; D008968:Molecular Conformation; D056004:Molecular Dynamics Simulation; D009038:Motion; D013261:Sterols / Q000737:chemistry*
chemical_list: D013261:Sterols; C569133:fibrosterol sulfate A