Yoon, D., et al., 500-fold enhancement of in situ (13)C liquid state NMR using gyrotron-driven temperature-jump DNP. J Magn Reson, 2016. 270: p. 142-6.
A 550-fold increase in the liquid state (13)C NMR signal of a 50muL sample was obtained by first hyperpolarizing the sample at 20K using a gyrotron (260GHz), then, switching its frequency in order to apply 100W for 1.5s so as to melt the sample, finally, turning off the gyrotron to acquire the (13)C NMR signal. The sample stays in its NMR resonator, so the sequence can be repeated with rapid cooling as the entire cryostat stays cold. DNP and thawing of the sample are performed only by the switchable and tunable gyrotron without external devices. Rapid transition from DNP to thawing in one second time scale was necessary especially in order to enhance liquid (1)H NMR signal.
Dynamics of 4-oxo-TEMPO-d16-(15)N nitroxide-propylene glycol system studied by ESR and ESE in liquid and glassy state in temperature range 10-295K
From The DNP-NMR Blog:
Dynamics of 4-oxo-TEMPO-d16-(15)N nitroxide-propylene glycol system studied by ESR and ESE in liquid and glassy state in temperature range 10-295K
Goslar, J., S.K. Hoffmann, and S. Lijewski, Dynamics of 4-oxo-TEMPO-d16-(15)N nitroxide-propylene glycol system studied by ESR and ESE in liquid and glassy state in temperature range 10-295K. J Magn Reson, 2016. 269: p. 162-75.
http://www.ncbi.nlm.nih.gov/pubmed/27323281
Ultra-low temperature MAS-DNP #DNPNMR
From The DNP-NMR Blog:
Ultra-low temperature MAS-DNP #DNPNMR
Lee, D., et al., Ultra-low temperature MAS-DNP. J. Magn. Reson., 2016. 264: p. 116-124.
http://www.sciencedirect.com/science/article/pii/S1090780715003092
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05-16-2016 05:53 PM
Low-temperature dynamic nuclear polarization with helium-cooled samples and nitrogen-driven magic-angle spinning
From The DNP-NMR Blog:
Low-temperature dynamic nuclear polarization with helium-cooled samples and nitrogen-driven magic-angle spinning
Thurber, K. and R. Tycko, Low-temperature dynamic nuclear polarization with helium-cooled samples and nitrogen-driven magic-angle spinning. J Magn Reson, 2016. 264: p. 99-106.
http://www.ncbi.nlm.nih.gov/pubmed/26920835
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04-11-2016 07:16 PM
High-Speed Frequency Modulation of a 460-GHz Gyrotron for Enhancement of 700-MHz DNP-NMR Spectroscopy
From The DNP-NMR Blog:
High-Speed Frequency Modulation of a 460-GHz Gyrotron for Enhancement of 700-MHz DNP-NMR Spectroscopy
Idehara, T., et al., High-Speed Frequency Modulation of a 460-GHz Gyrotron for Enhancement of 700-MHz DNP-NMR Spectroscopy. J Infrared Milli Terahz Waves, 2015: p. 1-11.
http://dx.doi.org/10.1007/s10762-015-0176-2
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07-01-2015 02:40 PM
Evidenceof Entropy-Driven Bistability through 15N NMR Analysisof a Temperature- and Solvent-Induced, ChiropticalSwitching Polycarbodiimide
Evidenceof Entropy-Driven Bistability through 15N NMR Analysisof a Temperature- and Solvent-Induced, ChiropticalSwitching Polycarbodiimide
James F. Reuther and Bruce M. Novak
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja4098803/aop/images/medium/ja-2013-098803_0002.gif
Journal of the American Chemical Society
DOI: 10.1021/ja4098803
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/ogd4bIIAgFU
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Journal club
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12-17-2013 12:56 AM
[NMR paper] Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Real-time NMR monitoring of protein-folding kinetics by a recycle flow system for temperature jump.
Anal Chem. 2013 Sep 12;
Authors: Yamasaki K, Obara Y, Hasegawa M, Tanaka H, Yamasaki T, Wakuda T, Okada M, Kohzuma T
Abstract
An NMR method was developed that allows for real-time monitoring of reactions (on the order of seconds) induced by temperature jump. In a recycle flow system, heating and cooling baths were integrated, with the latter...
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09-14-2013 03:02 PM
[NMR paper] Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
Related Articles Temperature-jump NMR study of protein folding: ribonuclease A at low pH.
J Biomol NMR. 1991 May;1(1):65-70
Authors: Akasaka K, Naito A, Nakatani H
The kinetic process of folding of bovine pancreatic ribonuclease A in a 2H2O environment at pH 1.2 was examined by a recently developed temperature-jump NMR method (Akasaka et al., (1990) Rev. Sci. Instrum. 61, 66-68). Upon temperature-jump down from 45 degrees C to 29 degrees C, which was attained within 6 s,...
500-fold enhancement of in situ (13)C liquid state NMR using gyrotron-driven temperature-jump DNP #DNPNMR
Linear Mode
