Resolution enhancement by homonuclear J decoupling in solid-state MAS NMR

Straus, Suzana K.; Bremi, Tobias; Ernst, R. R.

doi:10.1016/s0009-2614(96)01143-8

Cited by 54 publications

(104 citation statements)

References 10 publications

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“…This method substantially increases spectral resolution by decoupling scalar interactions in the indirect dimension. 31 In constant-time 2D 13 C- 13 C experiments, 28 sensitivity was found to be comparable to or better than that of dipolar methods, in part owing to the relatively large homonuclear scalar couplings (¾35-55 Hz) responsible for the coherence transfer. More recently, we showed that analogous 3D schemes for heteronuclear NCACO, NCOCA, and CANCO correlation spectroscopy work equally well, despite coherence transfers reliant upon even smaller heteronuclear 15 N- 13 C scalar couplings (J NC ).…”

Section: Introductionmentioning

confidence: 99%

J-based 2D homonuclear and heteronuclear correlation in solid-state proteins

Kaiser¹,

Lai²,

Polenova³

et al. 2007

Magn. Reson. Chem.

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Scalar-based two-dimensional heteronuclear experiments are reported for NCO and NCA chemical shift correlation in the solid state. In conjunction with homonuclear CACO correlation, these experiments form a useful set for tracing connectivities and assigning backbone resonances in solid-state proteins. The applicability of this approach is demonstrated on two proteins, the β 1 immunoglobulin binding domain of protein G at 9.4 T and reassembled thioredoxin at 14.1 T, using different decoupling conditions and MAS frequencies. These constant-time J-based correlation experiments exhibit increased resolution in the indirect dimension owing to homonuclear and heteronuclear decoupling, and because the indirect evolution and transfer periods are combined into a single constant time interval, this increased resolution is not obtained at the cost of sensitivity. These experiments are also shown to be compatible with in-phase anti-phase (IPAP) selection, giving increased resolution in the directly detected dimension.

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Section: Introductionmentioning

confidence: 99%

J-based 2D homonuclear and heteronuclear correlation in solid-state proteins

Kaiser¹,

Lai²,

Polenova³

et al. 2007

Magn. Reson. Chem.

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“…[11] This sequence provides an enhanced resolution in the Ca-Cx region (with Cx = C', Cb, Cg, etc.) by refocusing the J Ca-Cb and J Ca-C' scalar couplings in the indirect dimension (F1).…”

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confidence: 99%

Solid‐State NMR of Matrix Metalloproteinase 12: An Approach Complementary to Solution NMR

et al. 2007

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Data transfer. The solid‐state proton‐driven spin diffusion (PDSD) and J‐decoupled PDSD NMR spectra of the microcrystalline catalytic domain of matrix metalloproteinase 12 (MMP‐12, 17 kDa) have been recorded. It is shown that such spectra can be largely assigned in a few days by using the available liquid‐state assignment and validated with an independent sequential assignment based on 3D NCACX and NCOCX PDSD experiments. This demonstrates how quickly the liquid‐state assignment of comparably large protein can be transferred to the solid state.

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“…The second condition may be fulfilled by performing two-dimensional (2D) NMR experiments where one dimension separates and identifies the chemically distinct sites through their isotropic chemical shifts, while the other dimension yields the structural parameters (8). The first condition can be fulfilled by uniform 13 C and 15 N labeling of the proteins, which is used routinely now in solution NMR to determine the structure of globular proteins (9,10). In solidstate NMR, uniform 15 N labeling has also been utilized to obtain information such as the orientation of protein segments in the membrane bilayer (11).…”

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confidence: 99%

“…In solidstate NMR, uniform 15 N labeling has also been utilized to obtain information such as the orientation of protein segments in the membrane bilayer (11). However, uniform 13 C labeling of proteins leads to several spectroscopic difficulties for solidstate NMR. First, the one-bond 13 C-13 C J-couplings and the multispin dipolar couplings that are effective in fully 13 Clabeled proteins cause significant line broadening.…”

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confidence: 99%