Examination of Homogeneous Broadening in Solids via Rotationally Synchronized Spin-Echo NMR Spectroscopy

Cowans, Brett A.; Grutzner, John B.

doi:10.1006/jmra.1993.1242

Cited by 25 publications

(34 citation statements)

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“…Other sources might involve the anisotropic magnetic susceptibility (Cowans and Grutzner 1993;Garroway 1977;Vanderhart et al 1981). The estimated molecular weight at which solidstate NMR yields a more favourable resolution compared to solution-state NMR experiments therefore represents an upper limit that is implied by the current technology.…”

Section: Resultsmentioning

confidence: 99%

Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state

2010

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HNCO/HNCACO type correlation experiments are an alternative for assignment of backbone resonances in extensively deuterated proteins in the solid-state, given the fact that line widths on the order of 14-17 Hz are achieved in the carbonyl dimension without the need of high power decoupling. The achieved resolution demonstrates that MAS solid-state NMR on extensively deuterated proteins is able to compete with solution-state NMR spectroscopy if proteins are investigated with correlation times s c that exceed 25 ns.

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Section: Resultsmentioning

confidence: 99%

Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state

2010

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“…Specifically, the dephasing time T 2 0 that characterises the decay of transverse magnetisation during the spin-echo evolution time, , is usually considerably longer than the decay constant of the non-refocused NMR signal, T 2 Ł , which characterises the detected free-induction decay (FID). 49,50 For disordered systems, the difference between T 2 0 and T 2 Ł is principally a consequence of the refocusing by the spin echo of all terms that appear as offsets, e.g. a distribution of chemical shifts due to chemical disorder.…”

Section: Introductionmentioning

confidence: 99%

Low-load rotor-synchronised Hahn-echo pulse train (RS-HEPT)1H decoupling in solid-state NMR: factors affecting MAS spin-echo dephasing times

et al. 2007

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Transverse dephasing times T(2)' in spin-echo MAS NMR using rotor-synchronised Hahn-echo pulse-train (RS-HEPT) low-load (1)H decoupling are evaluated. Experiments were performed at 300 and 600 MHz for (13)CH-labelled L-alanine and (15)NH(delta)-labelled L-histidine.HCl.H(2)O, together with SPINEVOLUTION simulations for a ten-spin system representing the crystal structure environment of the (13)CH carbon in L-alanine. For 30 kHz MAS and nu(1)((1)H) = 100 kHz at 300 MHz, a RS-HEPT T(2)' value of 17 +/- 1 ms was obtained for (13)CH-labelled L-alanine which is approximately 50% of the XiX T(2)' value of 33 +/- 2 ms. Optimum RS-HEPT decoupling performance is observed for a relative phase of alternate RS-HEPT pi-pulses, Deltaphi = phi'- phi, between 40 and 60 degrees . For experiments at 600 MHz and 30 kHz MAS with (13)CH-labelled L-alanine, the best RS-HEPT (nu(1)((1)H) = 100 kHz) T(2)' value was 3 times longer than that observed for low-power continuously applied sequences with nu(1)((1)H) < or =40 kHz, i.e. corresponding to the same average power dissipated in the probe. A marked improvement in RS-HEPT (1)H decoupling is observed for increasing MAS frequency: at 55.6 kHz MAS, a best RS-HEPT T(2)' value of 34 +/- 5 ms was recorded for (13)CH-labelled L-alanine. Much improved RS-HEPT broadband performance was also observed at 55.6 kHz MAS as compared to 30 kHz MAS.

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“…ABMS cannot be suppressed simply by magic angle spinning. However, since the Hamiltonian for the ABMS interaction has a similar dependence as the isotropic chemical shifts on the nuclear spin part (Samoson et al 2001), application of a CPMG pulse train can induce significant line narrowing (Garroway 1977;Cowans et al 1993;Wiench et al 2008). The spin-echo FID yields a spike spectrum upon Fourier transformation, in which the distance between two spikes is determined by the CPMG frequency.…”

Section: Limits Of Resolutionmentioning

confidence: 99%

“…The spin-echo FID yields a spike spectrum upon Fourier transformation, in which the distance between two spikes is determined by the CPMG frequency. The isotropic chemical shift information can be reconstructed from the spikespectrum, provided the CPMG frequency is smaller than the frequency difference between two chemical shifts (Cowans et al 1993). Analogous methods have been found useful applications to enhance sensitivity for 29 Si (Wiench et al 2008;Bocan et al 2012).…”

Section: Limits Of Resolutionmentioning

confidence: 99%

Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes

et al. 2014

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Aggregates formed by amyloidogenic peptides and proteins and reconstituted membrane protein preparations differ significantly in terms of the spectral quality that they display in solid-state NMR experiments. Structural heterogeneity and dynamics can both in principle account for that observation. This perspectives article aims to point out challenges and limitations, but also potential opportunities in the investigation of these systems.

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Examination of Homogeneous Broadening in Solids via Rotationally Synchronized Spin-Echo NMR Spectroscopy

Cited by 25 publications

References 0 publications

Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state

Narrow carbonyl resonances in proton-diluted proteins facilitate NMR assignments in the solid-state

Low-load rotor-synchronised Hahn-echo pulse train (RS-HEPT)1H decoupling in solid-state NMR: factors affecting MAS spin-echo dephasing times

Dynamics in the solid-state: perspectives for the investigation of amyloid aggregates, membrane proteins and soluble protein complexes

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