Niedbalski, P., et al., Magnetic-Field-Dependent Lifetimes of Hyperpolarized 13C Spins at Cryogenic Temperature. The Journal of Physical Chemistry B, 2018. 122(6): p. 1898-1904.
Using a home-built cryogen-free dynamic nuclear polarization (DNP) system with a variable magnetic field capability, 13C spin–lattice T1 relaxation times of hyperpolarized [1-13C] carboxylates (sodium acetate, glycine, sodium pyruvate, and pyruvic acid) doped with trityl OX063 free radical were systematically measured for the first time at different field strengths up to 9 T at T = 1.8 K. Our data reveal that the 13C T1 values of these frozen hyperpolarized 13C samples vary drastically with the applied magnetic field B according to an apparent empirical power-law dependence (13C T1 ? B?, 2.3 < ? < 3.1), with relaxation values ranging from a few hundred seconds at 1 T to over 200,000 s at fields close to 9 T. This low temperature relaxation behavior can be ascribed approximately to a model that accounts for the combined effect of 13C–1H intramolecular dipolar interaction and the relaxation contribution from the paramagnetic impurities present in the DNP sample. Since the lifetime or T1 storage of the hyperpolarized state is intimately linked to DNP efficiency, these 13C relaxation data at cryogenic temperature have important theoretical and experimental implications as the DNP of 13C-labeled biomolecules is pushed to higher magnetic fields.
Spin polarization transfer mechanisms of SABRE: A magnetic field dependent study
From The DNP-NMR Blog:
Spin polarization transfer mechanisms of SABRE: A magnetic field dependent study
Pravdivtsev, A.N., et al., Spin polarization transfer mechanisms of SABRE: A magnetic field dependent study. J Magn Reson, 2015. 261: p. 73-82.
http://www.ncbi.nlm.nih.gov/pubmed/26529205
nmrlearner
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04-01-2016 09:27 PM
Room temperature hyperpolarization of nuclear spins in bulk
From The DNP-NMR Blog:
Room temperature hyperpolarization of nuclear spins in bulk
Tateishi, K., et al., Room temperature hyperpolarization of nuclear spins in bulk. Proc Natl Acad Sci U S A, 2014. 111(21): p. 7527-30.
http://www.ncbi.nlm.nih.gov/pubmed/24821773
nmrlearner
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08-19-2015 03:24 PM
Room temperature hyperpolarization of nuclear spins in bulk
From The DNP-NMR Blog:
Room temperature hyperpolarization of nuclear spins in bulk
Tateishi, K., et al., Room temperature hyperpolarization of nuclear spins in bulk. Proc. Nat. Aca. Sci. USA, 2014. 111(21): p. 7527-7530.
http://www.pnas.org/content/111/21/7527.abstract
Dynamic nuclear polarization (DNP), a means of transferring spin polarization from electrons to nuclei, can enhance the nuclear spin polarization (hence the NMR sensitivity) in bulk materials at most 660 times for 1H spins, using electron spins in thermal equilibrium as polarizing agents. By using electron spins...
nmrlearner
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07-12-2014 04:28 AM
Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse
From The DNP-NMR Blog:
Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse
Marco-Rius, I., et al., Hyperpolarized singlet lifetimes of pyruvate in human blood and in the mouse. NMR Biomed, 2013. 26(12): p. 1696-704.
http://www.ncbi.nlm.nih.gov/pubmed/23946252
nmrlearner
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03-19-2014 10:43 PM
[Question from NMRWiki Q&A forum] Are there ways to explain magnetic-field dependent chemical shift?
Are there ways to explain magnetic-field dependent chemical shift?
Hi everyone,
I was wondering whether anyone could help me to explain why the chemical shifts in my proton and carbon NMR results do not exactly match with those reported in the literature?The solvent used in my experiment is exactly the same as the one used in the literature of reference (CD3OD), however the frequency applied in my experiment was 500MHz as opposed to 400MHz by the study i am comparing my results with.
For example, in my proton NMR spectra, my results are usually 0.08 to 0.26 ppm higher than that in...
nmrlearner
News from other NMR forums
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08-05-2012 03:59 PM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR
Abstract X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100 K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down...
nmrlearner
Journal club
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08-13-2011 02:47 AM
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR.
J Biomol NMR. 2011 Aug 9;
Authors: Linden AH, Franks WT, Akbey U, Lange S, van Rossum BJ, Oschkinat H
X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100*K. Protein dynamics are poorly understood...
nmrlearner
Journal club
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08-10-2011 12:30 PM
[NMR paper] 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conf
1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H- and 13C-NMR investigation of redox-state-dependent and temperature-dependent conformation changes in horse cytochrome c.
Eur J Biochem. 1993 Feb 1;211(3):555-62
Authors: Turner DL, Williams RJ
The redox-state dependent changes in chemical shift, which have...