Sensitivity enhancement, assignment, and distance measurement in 13C solid-state NMR spectroscopy for paramagnetic systems under fast magic angle spinning

Wickramasinghe, Nalinda P.; Ishii, Yoshitaka

doi:10.1016/j.jmr.2006.05.008

Cited by 76 publications

(88 citation statements)

References 61 publications

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“…We also tested decoupling by fast MAS at 20-30 kHz, which was successfully employed in our recent studies for paramagnetic systems. [37][38][39] However, the resolution without 1 H RF decoupling is considerably limited for the diamagnetic polycrystalline proteins.…”

Section: Resultsmentioning

confidence: 99%

Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation

Wickramasinghe

Kotecha

Samoson

et al. 2007

Journal of Magnetic Resonance

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We discuss a simple approach to enhance sensitivity for 13 C high-resolution solid-state NMR for proteins in microcrystals by reducing 1 H T 1 relaxation times with paramagnetic relaxation reagents. It was shown that 1 H T 1 values can be reduced from 0.4-0.8 s to 60-70 ms for ubiquitin and lysozyme in D 2 O in the presence of 10 mM Cu(II)Na 2 EDTA without substantial degradation of the resolution in 13 C CPMAS spectra. Faster signal accumulation using the shorter 1 H T 1 attained by paramagnetic doping provided sensitivity enhancements of 1.4-2.9 for these proteins, reducing the experimental time for a given signal-to-noise ratio by a factor of 2.0-8.4. This approach presented here is likely to be applicable to various other proteins in order to enhance sensitivity in 13 C high-resolution solidstate NMR spectroscopy.

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Section: Resultsmentioning

confidence: 99%

Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation

Wickramasinghe

Kotecha

Samoson

et al. 2007

Journal of Magnetic Resonance

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119

110

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“…Mn also causes paramagnetic anisotropic shift dispersion in immobile solidstate samples because of its large electron spin quantum number and decreases the signal intensities because the efficiency of CP is reduced in addition to PRE (Wickramasinghe and Ishii 2006 ). We evaluated the influence of paramagnetic anisotropic shift dispersion by spin dynamics simulations, and the results are included in our experimental analysis (see SI text for further detail).…”

Section: Paramagnetic Signal Decaymentioning

confidence: 99%

Structure determination of uniformly 13C, 15N labeled protein using qualitative distance restraints from MAS solid-state 13C-NMR observed paramagnetic relaxation enhancement

et al. 2016

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Magic angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) is a powerful method for structure determination of insoluble biomolecules. However, structure determination by MAS solid-state NMR remains challenging because it is difficult to obtain a sufficient amount of distance restraints owing to spectral complexity. Collection of distance restraints from paramagnetic relaxation enhancement (PRE) is a promising approach to alleviate this barrier. However, the precision of distance restraints provided by PRE is limited in solid-state NMR because of incomplete averaged interactions and intermolecular PREs. In this report, the backbone structure of the B1 domain of streptococcal protein G (GB1) has been successfully determined by combining the CS-Rosetta protocol and qualitative PRE restraints. The derived structure has a Cα RMSD of 1.49 Å relative to the Xray structure. It is noteworthy that our protocol can determine the correct structure from only three cysteine-EDTA-Mn mutants because this number of PRE sites is insufficient when using a conventional structure calculation method based on restrained molecular dynamics and simulated annealing. This study shows that qualitative PRE restraints can be employed effectively for protein structure determination from a limited conformational sampling space using a protein fragment library. KeywordsSolid-state NMR Magic-angle spinning Protein structure Paramagnetic relaxation enhancement CS-Rosetta Electronic supplementary materialThe online version of this article

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“…In that case, MAS powder spectra feature numerous spinning sidebands. Such wide spectra are encountered when: (i) the nuclei are close either to unpaired electrons in paramagnetic samples [2][3][4][5][6][7][8][9][10][11][12] or to conduction electrons in electrical conductors, (ii) the nuclei are subject to large quadrupole interactions (I > 1/2) [13][14][15][16][17][18][19][20][21][22][23][24][25], or (iii) their chemical shift anisotropy (CSA) is large, particularly when the static magnetic field is high [26,27].…”

Section: Introductionmentioning

confidence: 99%

Broadband excitation in solid-state NMR using interleaved DANTE pulse trains with N pulses per rotor period

Trébosc

Lafon

et al. 2013

Journal of Magnetic Resonance

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N Broadband excitation DANTE MAS Paramagnetic samples a b s t r a c tWe analyze the direct excitation of wide one-dimensional spectra of nuclei with spin I = 1/2 or 1 in rotating solids submitted to pulse trains in the manner of Delays Alternating with Nutations for Tailored Excitation (DANTE), either with one short rotor-synchronized pulse of duration s p in each of K rotor periods For nuclei with I = 1 (e.g., for 14 N), the response to basic D K 1 pulse train is moreover affected by inhomogeneous decay due to 2nd-order quadrupole interactions, since these are not of rank 2 and therefore cannot be eliminated by spinning about the magic angle. For large quadrupole interactions, the signal decay produced by second-order quadrupole interaction can be minimized by (i) reducing the length of D K N pulse trains using N > 1, (ii) fast spinning, (iii) large rf-field, and (iv) using high magnetic fields to reduce the 2nd-order quadrupole interaction.

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Sensitivity enhancement, assignment, and distance measurement in 13C solid-state NMR spectroscopy for paramagnetic systems under fast magic angle spinning

Cited by 76 publications

References 61 publications

Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation

Sensitivity enhancement in 13C solid-state NMR of protein microcrystals by use of paramagnetic metal ions for optimizing 1H T1 relaxation

Structure determination of uniformly 13C, 15N labeled protein using qualitative distance restraints from MAS solid-state 13C-NMR observed paramagnetic relaxation enhancement

Broadband excitation in solid-state NMR using interleaved DANTE pulse trains with N pulses per rotor period

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