Solid state NMR studies of paramagnetic coordination complexes: A comparison of protons and deuterons in detection and decoupling

Li, Kai; Ryan, D.; Nakanishi, Kōji; McDermott, Ann E.

doi:10.1021/ja00131a011

Cited by 95 publications

(173 citation statements)

References 4 publications

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“…In these cases, 1 H linewidths improve very rapidly with increasing spinning rate. 42,43 Rotational resonance is another mechanism by which chemical shift differences can influence line shapes in magicangle spinning NMR. 40,44,45 This occurs if the difference in resonance frequencies ⌬ between two coupled spins matches to a small multiple n of the MAS rate.…”

Section: ͑9͒mentioning

confidence: 99%

Origins of linewidth in H1 magic-angle spinning NMR

Zorin

Brown

Hodgkinson

2006

The Journal of Chemical Physics

125

116

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A detailed study of the factors determining the linewidth (and hence resolution) in H1 solid-state magic-angle spinning NMR is described. Although it has been known from the early days of magic-angle spinning (MAS) that resolution of spectra from abundant nuclear spins, such as H1, increases approximately linearly with increasing sample rotation rate, the difficulty of describing the dynamics of extended networks of coupled spins has made it difficult to predict a priori the resolution expected for a given sample. Using recently developed, highly efficient methods of numerical simulation, together with experimental measurements on a variety of test systems, we propose a comprehensive picture of H1 resolution under MAS. The “homogeneous” component of the linewidth is shown to depend primarily on the ratio between an effective local coupling strength and the spin rate, modified by geometrical factors which loosely correspond to the “dimensionality” of the coupling network. The remaining “inhomogeneous” component of the natural linewidth is confirmed to have the same properties as in dilute-spin NMR. Variations in the NMR frequency due to chemical shift effects are shown to have minimal impact on H1 resolution. The implications of these results for solid-state NMR experiments involving H1 and other abundant-spin nuclei are discussed.

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Section: ͑9͒mentioning

confidence: 99%

Origins of linewidth in H1 magic-angle spinning NMR

Zorin

Brown

Hodgkinson

2006

The Journal of Chemical Physics

125

116

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“…Small paramagnetic molecules have been studied through magic angle spinning (MAS) SSNMR for decades (27-33). Paramagnetism in the solid state causes problems connected with the large shift anisotropy, inhomogeneous broadening (34), and the difficulties in obtaining efficient proton decoupling (30,32). Pioneering works have shown that paramagnetic proteins are also affordable by SSNMR by using either perdeuterated substrates (35) or selective labeling (36).…”

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confidence: 99%

“…Small paramagnetic molecules have been studied through magic angle spinning (MAS) SSNMR for decades (27)(28)(29)(30)(31)(32)(33). Paramagnetism in the solid state causes problems connected with the large shift anisotropy, inhomogeneous broadening (34), and the difficulties in obtaining efficient proton decoupling (30,32).…”

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confidence: 99%

Paramagnetic shifts in solid-state NMR of proteins to elicit structural information

Balayssac

Bertini

Bhaumik

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

141

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The recent observation of pseudocontact shifts (pcs) in 13 C highresolution solid-state NMR of paramagnetic proteins opens the way to their application as structural restraints. Here, by investigating a microcrystalline sample of cobalt(II)-substituted matrix metalloproteinase 12 [CoMMP-12 (159 AA, 17.5 kDa)], it is shown that a combined strategy of protein labeling and dilution of the paramagnetic species (i.e., 13 C-, 15 N-labeled CoMMP-12 diluted in unlabeled ZnMMP-12, and 13 C-, 15 N-labeled ZnMMP-12 diluted in unlabeled CoMMP-12) allows one to easily separate the pcs contributions originated from the protein internal metal (intramolecular pcs) from those due to the metals in neighboring proteins in the crystal lattice (intermolecular pcs) and that both can be used for structural purposes. It is demonstrated that intramolecular pcs are significant structural restraints helpful in increasing both precision and accuracy of the structure, which is a need in solid-state structural biology nowadays. Furthermore, intermolecular pcs provide unique information on positions and orientations of neighboring protein molecules in the solid phase.S olid-state NMR (SSNMR) on biomolecules is a rapidly growing technique, with an increased interest based on its ability to determine protein structures in the solid phase (1, 2) and to permit the study of noncrystalline biomolecular systems such as membrane proteins (3) and fibrils (4, 5).Limitations in biomolecular structural determination through SSNMR are due to the difficulties in obtaining a large number of restraints to be used for structural purposes (4, 6-9). Most of the structural information is obtained through distance restraints, analogous to nuclear Overhauser effects (NOE) in solution NMR, which in the solid state are obtained through experiments such as proton-driven spin diffusion (PDSD) (1, 6, 10), and CHHC (11), whereas specifically designed sequences can be applied on short peptides (4,(12)(13)(14). The ability to obtain a large number of distance restraints is hampered by the reduced resolution of SSNMR spectra, which increases the amount of ambiguities in the assigned restraints (15), whereas relayed transfer (10, 16) and the effects of the dipolar truncation (17) affect the accuracy of these restraints. These problems have been tackled by working on samples prepared with selective labeling schemes (1, 6) and, more recently, on uniformly labeled proteins with the help of software able to provide automated PDSD/ CHHC assignment and on dealing with a large number of ambiguous restraints (10,15,18). However, even when additional dihedral angle restraints from backbone chemical shiftsthrough Chemical Shift Index (CSI) (19) or TALOS (20) programs-are used, the size of the affordable proteins has been, up to now, limited to small systems (Ͻ100 aa) (10,15,18). In this work, we show how SSNMR paramagnetic restraints such as pseudocontact shifts (pcs) can be used as additional sources of restraints for protein structural determination, even providing information abou...

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“…Although Bloembergen's systematic study [5] of the solid-state proton NMR spectrum of CuSO 4 · 5H 2 O dates back to the 1950s, the applications of solid-state NMR to paramagnetic samples remained relatively unexplored until a number of papers [6][7][8][9][10][11][12] appeared around the late 1980s, coinciding with wider availability of robust and relatively high speed commercial magic-angle spinning (MAS) probes. It was discovered that high resolution proton MAS experiments were aided by the larger paramagnetic shifts which turned homonuclear couplings into inhomogeneous broadenings [13,14]. As MAS spinning speeds increased it became possible to develop solid-state NMR analogs of many solution-state paramagnetic NMR (pNMR) experiments [15].…”

Section: Introductionmentioning

confidence: 99%