ArticleChemphyschem : a European journal of chemical physics and physical chemistry2009
Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements.
Article in Chemphyschem : a European journal of chemical physics and physical chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Dihedral Angle Measurements for Structure Determination by Biomolecular Solid-State NMR Spectroscopy.Frontiers in molecular biosciences · 2021Review
- Modular, triple-resonance, transmission line DNP MAS probe for 500 MHz/330 GHz.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2019Article
- Spinning-rate encoded chemical shift correlations from rotational resonance solid-state NMR experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2013Article
- Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR.Biochemistry · 2010Article
- High-resolution solid-state NMR structure of alanyl-prolyl-glycine.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
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Abstract
Rotational resonance width (R(2)W) magic-angle spinning (MAS) NMR experiments are performed to measure (13)C-(13)C distances in the hydrophobic core of the microcrystalline model protein G(Beta1). Such inter-residue distances are of particular value in NMR structure determinations. The experiments are done at a Larmor frequency of 750 MHz (1)H where the contribution of (13)C chemical shift anisotropy (CSA) to the R(2) transfer mechanism is significant. To minimize line broadening in the 2D spectra, we employ a combination of even/odd isotopic labeling with [1,3-(13)C] glycerol, and J-decoupling in the indirect dimension. This results in high-precision distance measurements between aromatic side chains of three tyrosine residues and distant methyl groups in the hydrophobic core of the protein. Even in the absence of information on the relative orientation of the shift tensors, we obtain relatively high precision data, which can be further improved by additional constraints on the tensor orientations.
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