Polarization transfer from hyperpolarized water through proton exchange is used to enhance the NMR signals of amide protons of the Ribonuclease Sa protein. Spectra of the refolding protein are measured within 6 s after dilution of the denaturant urea, at urea-dependent folding rates adjusted in the range of 0.3-0.8 s^(-1). Peak patterns including a mixture of folded and unfolded protein at different ratios are observed. The changes in the observed signals indicate that each spectrum accesses a...
Hyperpolarized water through dissolution dynamic nuclear polarization with UV-generated radicals #DNPNMR
From The DNP-NMR Blog:
Hyperpolarized water through dissolution dynamic nuclear polarization with UV-generated radicals #DNPNMR
Pinon, Arthur C., Andrea Capozzi, and Jan Henrik Ardenkjær-Larsen. “Hyperpolarized Water through Dissolution Dynamic Nuclear Polarization with UV-Generated Radicals.” Communications Chemistry 3, no. 1 (December 2020): 57.
https://doi.org/10.1038/s42004-020-0301-6.
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08-07-2020 08:10 PM
Modeling of Polarization Transfer Kinetics in Protein Hydration Using Hyperpolarized Water
From The DNP-NMR Blog:
Modeling of Polarization Transfer Kinetics in Protein Hydration Using Hyperpolarized Water
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Kim, J., M. Liu, and C. Hilty, Modeling of Polarization Transfer Kinetics in Protein Hydration Using Hyperpolarized Water. The Journal of Physical Chemistry B, 2017. 121(27): p. 6492-6498.
http://dx.doi.org/10.1021/acs.jpcb.7b03052
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11-01-2017 07:49 PM
Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase
From The DNP-NMR Blog:
Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase
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Wang, Y., M. Ragavan, and C. Hilty, Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase. J. Biomol. NMR, 2016. 65(1): p. 41-48.
http://dx.doi.org/10.1007/s10858-016-0037-x
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05-15-2017 04:34 PM
Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase
Site specific polarization transfer from a hyperpolarized ligand of dihydrofolate reductase
Abstract
Proteinâ??ligand interaction is often characterized using polarization transfer by the intermolecular nuclear Overhauser effect (NOE). For such NOE experiments, hyperpolarization of nuclear spins presents the opportunity to increase the spin magnetization, which is transferred, by several orders of magnitude. Here, folic acid, a ligand of dihydrofolate reductase (DHFR), was hyperpolarized on 1H spins using dissolution dynamic nuclear polarization...
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05-18-2016 09:53 PM
Polarization Transfer from Ligands Hyperpolarized by Dissolution Dynamic Nuclear Polarization for Screening in Drug Discovery
From The DNP-NMR Blog:
Polarization Transfer from Ligands Hyperpolarized by Dissolution Dynamic Nuclear Polarization for Screening in Drug Discovery
Min, H., G. Sekar, and C. Hilty, Polarization Transfer from Ligands Hyperpolarized by Dissolution Dynamic Nuclear Polarization for Screening in Drug Discovery. ChemMedChem, 2015. 10(9): p. 1559-63.
http://www.ncbi.nlm.nih.gov/pubmed/26315550
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10-05-2015 07:08 PM
[NMR paper] Probing membrane protein structure using water polarization transfer solid-state NMR.
Probing membrane protein structure using water polarization transfer solid-state NMR.
Related Articles Probing membrane protein structure using water polarization transfer solid-state NMR.
J Magn Reson. 2014 Aug 25;
Authors: Williams JK, Hong M
Abstract
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected (1)H polarization transfer from water to biomolecules is a versatile approach for studying water-protein,...
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09-18-2014 01:33 PM
[NMR paper] Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Probing Membrane Protein Structure Using Water Polarization Transfer Solid-State NMR
Publication date: Available online 25 August 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Jonathan K. Williams , Mei Hong</br>
Water plays an essential role in the structure and function of proteins, lipid membranes and other biological macromolecules. Solid-state NMR heteronuclear-detected 1H polarization transfer from water to biomolecules is a versatile approach for studying water-protein, water-membrane, and water-carbohydrate interactions in biology. We review...
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08-26-2014 01:14 AM
[NMR paper] Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in
Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
Related Articles Hydration water molecules of nucleotide-free RNase T1 studied by NMR spectroscopy in solution.
J Biomol NMR. 1998 Jan;11(1):1-15
Authors: Pfeiffer S, Spitzner N, Löhr F, Rüterjans H
The hydration of uncomplexed RNase T1 was investigated by NMR spectroscopy at pH 5.5 and 313 K. Two-dimensional heteronuclear NOE and ROE difference experiments were employed to determine the spatial proximity and the residence times of water molecules at...
2D NMR spectroscopy of refolding RNase Sa using polarization transfer from hyperpolarized water
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