ArticleJournal of biomolecular NMR2012
Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.
Article in Journal of biomolecular NMR, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed.
- Collecting Large Datasets of Unambiguous Structural Restraints for Protein Structure Determination by 4D Proton-Detected Solid-State NMR.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Measuring long-range contacts in a fully protonated protein at 105 kHz magic angle spinning.Journal of biomolecular NMR · 2025Article
- Characterization of intrinsically disordered regions through scalar coupling-based solid-state NMR experiments.Biophysics reports · 2025Article
- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Cross polarization stability in multidimensional NMR spectroscopy of biological solids.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Homonuclear Simplified Preservation of Equivalent Pathways Spectroscopy.The journal of physical chemistry letters · 2024Article
- 5D solid-state NMR spectroscopy for facilitated resonance assignment.Journal of biomolecular NMR · 2023Article
- Article
- Great Offset Difference Internuclear Selective Transfer.The journal of physical chemistry letters · 2023Article
- ssPINE: Probabilistic Algorithm for Automated Chemical Shift Assignment of Solid-State NMR Data from Complex Protein Systems.Membranes · 2022Article
- Divide and Conquer: A Tailored Solid-state NMR Approach to Study Large Membrane Protein Complexes.Angewandte Chemie (International ed. in English) · 2022Article
- Modest Offset Difference Internuclear Selective Transfer via Homonuclear Dipolar Coupling.The journal of physical chemistry letters · 2022Article
- Close correlation between thiolate basicity and certain NMR parameters in cysteine and cystine microspecies.PloS one · 2022Article
- Protein resonance assignment by solid-state NMR based onJournal of biomolecular NMR · 2021Article
- Sensitivity-Enhanced Solid-State NMR Detection of Structural Differences and Unique Polymorphs in Pico- to Nanomolar Amounts of Brain-Derived and Synthetic 42-Residue Amyloid-β Fibrils.Journal of the American Chemical Society · 2021Article
- Heteronuclear and homonuclear radio-frequency-driven recoupling.Magnetic resonance (Gottingen, Germany) · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- Membrane Protein Structure Determination and Characterisation by Solution and Solid-State NMR.Biology · 2020Review
- Tailoring NMR experiments for structural characterization of amorphous biological solids: A practical guide.Solid state nuclear magnetic resonance · 2020Review
2 more citing papers are in PubMed but not listed here.
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10 authors.
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Abstract
Solid-state NMR has emerged as an important tool for structural biology and chemistry, capable of solving atomic-resolution structures for proteins in membrane-bound and aggregated states. Proton detection methods have been recently realized under fast magic-angle spinning conditions, providing large sensitivity enhancements for efficient examination of uniformly labeled proteins. The first and often most challenging step of protein structure determination by NMR is the site-specific resonance assignment. Here we demonstrate resonance assignments based on high-sensitivity proton-detected three-dimensional experiments for samples of different physical states, including a fully-protonated small protein (GB1, 6 kDa), a deuterated microcrystalline protein (DsbA, 21 kDa), a membrane protein (DsbB, 20 kDa) prepared in a lipid environment, and the extended core of a fibrillar protein (α-synuclein, 14 kDa). In our implementation of these experiments, including CONH, CO(CA)NH, CANH, CA(CO)NH, CBCANH, and CBCA(CO)NH, dipolar-based polarization transfer methods have been chosen for optimal efficiency for relatively high protonation levels (full protonation or 100 % amide proton), fast magic-angle spinning conditions (40 kHz) and moderate proton decoupling power levels. Each H-N pair correlates exclusively to either intra- or inter-residue carbons, but not both, to maximize spectral resolution. Experiment time can be reduced by at least a factor of 10 by using proton detection in comparison to carbon detection. These high-sensitivity experiments are especially important for membrane proteins, which often have rather low expression yield. Proton-detection based experiments are expected to play an important role in accelerating protein structure elucidation by solid-state NMR with the improved sensitivity and resolution.
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