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Bertini, I.* ; Luchinat, C.* ; Parigi, G.* ; Ravera, E.* ; Reif, B.* ; Turano, P.*

Solid-state NMR of proteins sedimented by ultracentrifugation.

Proc. Natl. Acad. Sci. U.S.A. 108, 10396-10399 (2011)
DOI Verlagsversion bestellen
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.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
ISSN (print) / ISBN 0027-8424
e-ISSN 1091-6490
Quellenangaben Band: 108, Heft: 26, Seiten: 10396-10399 Artikelnummer: , Supplement: ,
Verlag National Academy of Sciences
Begutachtungsstatus Peer reviewed