title: Probing molecular motion by double-quantum (13C,13C) solid-state NMR spectroscopy: application to ubiquitin.
abstract: We demonstrate the use of two-dimensional ((13)C,(13)C) double-quantum spectroscopy to detect molecular dynamics by solid-state NMR. Data collected on tyrosine-ethylester (TEE) are in line with previously determined ((1)H,(13)C) order parameters. Application of these experiments to microcrystalline ubiquitin reveals the presence of dynamics on millisecond or faster time scales and differences in local mobility depending on microcrystal preparation. In addition, solid-state NMR-based structure calculation indicates conformational variability of loop regions between different solid-phase ubiquitin preparations. Our data relate preparation-dependent changes observed in NMR spectral parameters such as chemical shifts and through-space correlations to differences in ubiquitin dynamics and conformation and suggest a prominent role of molecular mobility in microcrystalline ubiquitin.
authors.affiliation: Department for NMR-based Structural Biology, Max-Planck-Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Robert
authors.initials: R
authors.lastname: Schneider
authors.forename: Karsten
authors.initials: K
authors.lastname: Seidel
authors.forename: Manuel
authors.initials: M
authors.lastname: Etzkorn
authors.forename: Adam
authors.initials: A
authors.lastname: Lange
authors.forename: Stefan
authors.initials: S
authors.lastname: Becker
authors.forename: Marc
authors.initials: M
authors.lastname: Baldus
mesh_terms: D011232:Chemical Precipitation; D008958:Models, Molecular; D009068:Movement; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011092:Polyethylene Glycols / Q000737:chemistry; D011487:Protein Conformation; D025801:Ubiquitin / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D025801:Ubiquitin; D011092:Polyethylene Glycols