Abstract We have recently proposed sedimented solute NMR (SedNMR) as a solid-state method to access biomolecules without the need of crystallization or other sample manipulation. The drawback of SedNMR is that samples are intrinsically diluted and this is detrimental for the signal intensity. Ultracentrifugal devices can be used to increase the amount of sample inside the rotor, overcoming the intrinsic sensitivity limitation of the method. We designed two different devices and we here report the directions for using such devices and the relevant equations for determining the parameters for sedimentation.
Content Type Journal Article
Category Communication
Pages 1-5
DOI 10.1007/s10858-012-9657-y
Authors
Ivano Bertini, Center for Magnetic Resonance (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
Frank Engelke, Bruker Biospin GmbH, Silberstreifen 4, 76287 Rheinstetten, Germany
Leonardo Gonnelli, Center for Magnetic Resonance (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
Benno Knott, Bruker Biospin GmbH, Silberstreifen 4, 76287 Rheinstetten, Germany
Claudio Luchinat, Center for Magnetic Resonance (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
David Osen, Bruker Biospin GmbH, Silberstreifen 4, 76287 Rheinstetten, Germany
Enrico Ravera, Center for Magnetic Resonance (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, FI, Italy
Solid-state NMR of proteins sedimented by ultracentrifugation [Chemistry]
Solid-state NMR of proteins sedimented by ultracentrifugation
Bertini, I., Luchinat, C., Parigi, G., Ravera, E., Reif, B., Turano, P....
Date: 2011-06-28
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...
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Solid-state NMR of proteins sedimented by ultracentrifugation.
Solid-state NMR of proteins sedimented by ultracentrifugation.
Solid-state NMR of proteins sedimented by ultracentrifugation.
Proc Natl Acad Sci U S A. 2011 Jun 13;
Authors: Bertini I, Luchinat C, Parigi G, Ravera E, Reif B, Turano P
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...
On the use of ultracentrifugal devices for sedimented solute NMR
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