ArticleAnnual reports on NMR spectroscopy2016
Orphan spin polarization: A catalyst for high-throughput solid-state NMR spectroscopy of proteins.
Article in Annual reports on NMR spectroscopy, 2016. 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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Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Predicting Ti-49 NMR Chemical Shift With New NMR-DKH Basis Set.Journal of computational chemistry · 2025Article
- Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy: Advances in Methodology and Applications.Chemical reviews · 2023Review
- PHRONESIS: A One-Shot Approach for Sequential Assignment of Protein Resonances by Ultrafast MAS Solid-State NMR Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2022Article
- Multi-receiver solid-state NMR using polarization optimized experiments (POE) at ultrafast magic angle spinning.Journal of biomolecular NMR · 2020Article
- Proton-detected polarization optimized experiments (POE) using ultrafast magic angle spinning solid-state NMR: Multi-acquisition of membrane protein spectra.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Hybridization of TEDOR and NCX MAS solid-state NMR experiments for simultaneous acquisition of heteronuclear correlation spectra and distance measurements.Journal of biomolecular NMR · 2019Article
- Probing membrane protein ground and conformationally excited states using dipolar- and J-coupling mediated MAS solid state NMR experiments.Methods (San Diego, Calif.) · 2018Review
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2 authors at 1 institution in 1 country.
Funding
Abstract
Magic angle spinning solid-state NMR (MAS ssNMR) spectroscopy is a powerful method for structure determination of biomacromolecules that are recalcitrant to crystallization (membrane proteins and fibrils). Conventional multidimensional ssNMR methods acquire one experiment at a time. This approach is time consuming and discards orphan (unused) spin operators. Relatively low sensitivity and poor resolution of protein samples require long acquisition times for multidimensional ssNMR experiments. Here, we describe our recent progress in the development of multiple acquisition solid-state NMR methods for protein structure determination. A family of experiments called Polarization Optimized Experiments (POE) were designed, in which we utilized the orphan spin operators that are discarded in classical multidimensional NMR experiments, recovering them to allow simultaneous acquisition of multiple 2D and 3D experiments, all while using conventional probes with spectrometers equipped with one receiver. Three strategies namely, DUMAS, MEIOSIS, and MAeSTOSO were used for the concatenation of various 2D and 3D experiments. These methods open up new avenues for reducing the acquisition times of multidimensional experiments for biomolecular ssNMR spectroscopy.
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