ArticleJournal of biomolecular NMR2015
Six- and seven-dimensional experiments by combination of sparse random sampling and projection spectroscopy dedicated for backbone resonance assignment of intrinsically disordered proteins.
Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Ultra-Wideline 2D Correlations Among Low-γ Species in Solid-State NMR via the Progressive Saturation of a Common Proton Reservoir.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- High-dimensional solid-state NMR facilitated by transverse-mixing optimal control.Research square · 2025Article
- Atomic-resolution chemical characterization of (2x)72-kDa tryptophan synthase via four- and five-dimensionalProceedings of the National Academy of Sciences of the United States of America · 2022Article
- XLSY: Extra-Large NMR Spectroscopy.Angewandte Chemie (International ed. in English) · 2018Article
- Reconstruction of non-uniformly sampled five-dimensional NMR spectra by signal separation algorithm.Journal of biomolecular NMR · 2017Article
- Increasing the Chemical-Shift Dispersion of Unstructured Proteins with a Covalent Lanthanide Shift Reagent.Angewandte Chemie (International ed. in English) · 2016Article
- Five and four dimensional experiments for robust backbone resonance assignment of large intrinsically disordered proteins: application to Tau3x protein.Journal of biomolecular NMR · 2016Article
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2 authors.
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Abstract
Two novel six- and seven-dimensional NMR experiments are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in four indirectly detected dimensions and synchronous sampling in the additional dimensions using projection spectroscopy principle. The resulted data sets could be processed as five-dimensional data using existing software. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel experiments were successfully tested using 1 mM sample of α-synuclein on 600 and 800 MHz NMR spectrometers equipped with standard room temperature probes. The experiments allowed backbone assignment from a 1-day acquisition.
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