Protein Folding Studied by Dissolution Dynamic Nuclear Polarization

Chen, Hsueh‐Ying; Ragavan, Mukundan; Hilty, Christian

doi:10.1002/ange.201301851

Cited by 29 publications

(28 citation statements)

References 24 publications

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“…Additional applications of more biophysical nature include real-time enzyme kinetics [60], studies of biosynthetic pathways [60], detection of poorly-populated reaction intermediates [61], and ligand-detected protein-ligand interactions [62]. Recently, the pH-jump-induced refolding of the hyperpolarized ribosomal protein L23 was studied in real time by monitoring the time course of the 13 C NMR signal intensities [63]. …”

Section: Dissolution Dynamic Nuclear Polarizationmentioning

confidence: 99%

Sensitivity enhancement in solution NMR: Emerging ideas and new frontiers

Lee

Okuno

Cavagnero

2014

Journal of Magnetic Resonance

154

163

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Modern NMR spectroscopy has reached an unprecedented level of sophistication in the determination of biomolecular structure and dynamics at atomic resolution in liquids. However, the sensitivity of this technique is still too low to solve a variety of cutting-edge biological problems in solution, especially those that involve viscous samples, very large biomolecules or aggregation-prone systems that need to be kept at low concentration. Despite the challenges, a variety of efforts have been carried out over the years to increase sensitivity of NMR spectroscopy in liquids. This review discusses basic concepts, recent developments and future opportunities in this exciting area of research.

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Section: Dissolution Dynamic Nuclear Polarizationmentioning

confidence: 99%

Sensitivity enhancement in solution NMR: Emerging ideas and new frontiers

Lee

Okuno

Cavagnero

2014

Journal of Magnetic Resonance

154

163

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“…1,2 This offers a means to increase the sensitivity by several orders of magnitude. Molecular probes and nuclear spins of all kinds ( 6 Li, 13 C, 15 N, 89 Y, and 129 Xe) 3−6 may be enhanced in this fashion and then transferred and injected in vitro or infused in vivo in view of performing an ever-expanding range of studies, from the early detection of prostate cancer 7,8 to the real-time observation of metal−ligand complexation, 5 protein folding, 9 and polymerization. 10 Although spectacular enhancement factors can be achieved by D-DNP, applications are inexorably limited by the lifetime of the hyperpolarized magnetization, which is usually determined by the relaxation time T 1 .…”

Section: ■ Introductionmentioning

confidence: 99%

Hyperpolarization of Deuterated Metabolites via Remote Cross-Polarization and Dissolution Dynamic Nuclear Polarization

et al. 2014

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In deuterated molecules such as [1-(13)C]pyruvate-d3, the nuclear spin polarization of (13)C nuclei can be enhanced by combining Hartmann-Hahn cross-polarization (CP) at low temperatures (1.2 K) with dissolution dynamic nuclear polarization (D-DNP). The polarization is transferred from remote solvent protons to the (13)C spins of interest. This allows one not only to slightly reduce build-up times but also to increase polarization levels and extend the lifetimes T1((13)C) of the enhanced (13)C polarization during and after transfer from the polarizer to the NMR or MRI system. This extends time scales over which metabolic processes and chemical reactions can be monitored.

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“…The production of 13 C-hyperpolarized metabolites has opened the way to a broad range of novel experiments, such as the detection of intermediates in fast chemical reactions3 the observation of protein folding in real time4 or the detection and monitoring of cancer in humans5. In d-DNP experiments, the 13 C metabolites are usually polarized at low temperatures (1.2< T <4.2 K) and moderate fields (usually 3.35< B 0 <6.7 T) either directly6 or indirectly78910 by 1 H→ 13 C cross-polarization (CP)1112.…”

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confidence: 99%

Transportable hyperpolarized metabolites

et al. 2017

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Nuclear spin hyperpolarization of 13C-labelled metabolites by dissolution dynamic nuclear polarization can enhance the NMR signals of metabolites by several orders of magnitude, which has enabled in vivo metabolic imaging by MRI. However, because of the short lifetime of the hyperpolarized magnetization (typically <1 min), the polarization process must be carried out close to the point of use. Here we introduce a concept that markedly extends hyperpolarization lifetimes and enables the transportation of hyperpolarized metabolites. The hyperpolarized sample can thus be removed from the polarizer and stored or transported for use at remote MRI or NMR sites. We show that hyperpolarization in alanine and glycine survives 16 h storage and transport, maintaining overall polarization enhancements of up to three orders of magnitude.

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Protein Folding Studied by Dissolution Dynamic Nuclear Polarization

Cited by 29 publications

References 24 publications

Sensitivity enhancement in solution NMR: Emerging ideas and new frontiers

Sensitivity enhancement in solution NMR: Emerging ideas and new frontiers

Hyperpolarization of Deuterated Metabolites via Remote Cross-Polarization and Dissolution Dynamic Nuclear Polarization

Transportable hyperpolarized metabolites

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