ArticleJournal of biomolecular NMR2017
Joint non-uniform sampling of all incremented time delays for quicker acquisition in protein relaxation studies.
Article in Journal of biomolecular NMR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- Fast Ultra-SelectiveAngewandte Chemie (International ed. in English) · 2026Article
- Magnetstein: An Open-Source Tool for Quantitative NMR Mixture Analysis Robust to Low Resolution, Distorted Lineshapes, and Peak Shifts.Analytical chemistry · 2024Article
- Deeper Insight into Photopolymerization: The Synergy of Time-Resolved Nonuniform Sampling and Diffusion NMR.Journal of the American Chemical Society · 2022Article
- A simple approach for reconstruction of non-uniformly sampled pseudo-3D NMR data for accurate measurement of spin relaxation parameters.Journal of biomolecular NMR · 2021Article
- Rapid measurement of heteronuclear transverse relaxation rates using non-uniformly sampledMagnetic resonance (Gottingen, Germany) · 2021Article
- Accelerating Restricted Diffusion NMR Studies with Time-Resolved and Ultrafast Methods.Analytical chemistry · 2020Article
- Accelerating 2D NMR relaxation dispersion experiments using iterated maps.Journal of biomolecular NMR · 2019Article
- Non-uniform sampling in biomolecular NMR.Journal of biomolecular NMR · 2017Article
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4 authors.
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Abstract
NMR relaxometry plays crucial role in studies of protein dynamics. The measurement of longitudinal and transverse relaxation rates of [Formula: see text]N is the main source of information on backbone motions. However, even the most basic approach exploiting a series of [Formula: see text]N HSQC spectra can require several hours of measurement time. Standard non-uniform sampling (NUS), i.e. random under-sampling of indirect time domain, typically cannot reduce this by more than 2-4[Formula: see text] due to relatively low "compressibility" of these spectra. In this paper we propose an extension of NUS to relaxation delays. The two-dimensional space of [Formula: see text]/[Formula: see text] is sampled in a way similar to NUS of [Formula: see text]/[Formula: see text] domain in 3D spectra. The signal is also processed in a way similar to that known from 3D NUS spectra i.e. using one of the most popular compressed sensing algorithms, iterative soft thresholding. The 2D Fourier transform matrix is replaced with mixed inverse Laplace-Fourier transform matrix. The peak positions in resulting 3D spectrum are characterized by two frequency coordinates and relaxation rate and thus no additional fitting of exponential curves is required. The method is tested on three globular proteins, providing satisfactory results in a time corresponding to acquisition of two conventional [Formula: see text]N HSQC spectra.
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