Published in

National Academy of Sciences, Proceedings of the National Academy of Sciences, 26(108), p. 10396-10399, 2011

DOI: 10.1073/pnas.1103854108

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Solid-state NMR of proteins sedimented by ultracentrifugation

Journal article published in 2011 by Ivano Bertini, Claudio Luchinat ORCID, Giacomo Parigi, Enrico Ravera, Bernd Reif ORCID, Paola Turano
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.