ArticleCommunications chemistry2021
Residue-resolved monitoring of protein hyperpolarization at sub-second time resolution.
Article in Communications chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- The Core-Shell Conformational Space of Compartmentalized Single-Chain Nanoparticles by Paramagnetic and Hyperpolarized NMR Spectroscopy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Hyperpolarized NMR Reveals Low-Populated Folding Intermediates in DNA.Journal of the American Chemical Society · 2025Article
- Deep Learning for Hyperpolarized NMR of Intrinsically Disordered Proteins without Resolution Loss: Access to Short-Lived Intermediates.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Ultrafast Nuclear Magnetic Resonance as a Tool to Detect Rapid Chemical Change in Solution.ACS physical chemistry Au · 2024Review
- Frémy's Salt as a Low-Persistence Hyperpolarization Agent: Efficient Dynamic Nuclear Polarization Plus Rapid Radical Scavenging.Journal of the American Chemical Society · 2022Article
- Nuclear Overhauser spectroscopy in hyperpolarized water - chemicalChemical communications (Cambridge, England) · 2022Article
- Toward protein NMR at physiological concentrations by hyperpolarized water-Finding and mapping uncharted conformational spaces.Science advances · 2022Article
- Hyperpolarized water as universal sensitivity booster in biomolecular NMR.Nature protocols · 2022Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Signal-enhancement techniques for NMR spectroscopy are important to amplify the weak resonances provided by nuclear spins. Recently, 'hyperpolarization' techniques have been intensively investigated. These provide nuclear spin states far from equilibrium yielding strong signal boosts up to four orders of magnitude. Here we propose a method for real-time NMR of 'hyperpolarized' proteins at residue resolution. The approach is based on dissolution dynamic nuclear polarization (d-DNP), which enables the use of hyperpolarized buffers that selectively boost NMR signals of solvent-exposed protein residues. The resulting spectral sparseness and signal enhancements enable recording of residue-resolved spectra at a 2 Hz sampling rate. Thus, we monitor the hyperpolarization level of different protein residues simultaneously under near-physiological conditions. We aim to address two points: 1) NMR experiments are often performed under conditions that increase sensitivity but are physiologically irrelevant; 2) long signal accumulation impedes fast real-time monitoring. Both limitations are of fundamental relevance to ascertain pharmacological relevance and study protein kinetics.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.