title: Solid-state NMR of proteins sedimented by ultracentrifugation.
abstract: Relatively large proteins in solution, spun in NMR rotors for solid samples at typical ultracentrifugation speeds, sediment at the rotor wall. The sedimented proteins provide high-quality solid-state-like NMR spectra suitable for structural investigation. The proteins fully revert to the native solution state when spinning is stopped, allowing one to study them in both conditions. Transiently sedimented proteins can be considered a novel phase as far as NMR is concerned. NMR of transiently sedimented molecules under fast magic angle spinning has the advantage of overcoming protein size limitations of solution NMR without the need of sample crystallization/precipitation required by solid-state NMR.
authors.affiliation: Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy. ivanobertini@cerm.unifi.it
authors.forename: Ivano
authors.initials: I
authors.lastname: Bertini
authors.forename: Claudio
authors.initials: C
authors.lastname: Luchinat
authors.forename: Giacomo
authors.initials: G
authors.lastname: Parigi
authors.forename: Enrico
authors.initials: E
authors.lastname: Ravera
authors.forename: Bernd
authors.initials: B
authors.lastname: Reif
authors.forename: Paola
authors.initials: P
authors.lastname: Turano
mesh_terms: D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000032:analysis*; D014461:Ultracentrifugation / Q000379:methods*
chemical_list: D011506:Proteins