Nuclear spin relaxation and chemical exchange effects in the19F nuclear magnetic resonance spectrum of the hexafluoroniobate ion

1968 ◽  
Vol 14 (4) ◽  
pp. 301-309 ◽  
Author(s):  
D.W. Aksnes ◽  
Sheila M. Hutchison ◽  
K.J. Packer
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Spectrum ◽  
Spin Relaxation ◽  
Nuclear Spin ◽  
Resonance Spectrum ◽  
Chemical Exchange ◽  
Nuclear Spin Relaxation ◽  
Exchange Effects ◽  
Nuclear Magnetic

scholarly journals Nuclear magnetic resonance and nuclear spin relaxation in AlAs quantum well probed by ESR

2016 ◽  
Vol 94 (24) ◽  
Author(s):  
A. V. Shchepetilnikov ◽  
D. D. Frolov ◽  
Yu. A. Nefyodov ◽  
I. V. Kukushkin ◽  
D. S. Smirnov ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Quantum Well ◽  
Spin Relaxation ◽  
Nuclear Spin ◽  
Nuclear Spin Relaxation ◽  
Nuclear Magnetic

The 31P nuclear magnetic resonance spectrum of cows' milk

1985 ◽  
Vol 52 (1) ◽  
pp. 47-54 ◽  
Author(s):  
Peter S. Belton ◽  
Richard L. J. Lyster ◽  
Colin P. Richards
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Nuclear Magnetic Resonance Spectrum ◽  
Resonance Spectrum ◽  
Chemical Exchange ◽  
Chemical Shifts ◽  
Casein Micelle ◽  
Liquid Milk ◽  
Similar Solutions ◽  
Nuclear Magnetic

SUMMARYThe 31P nuclear magnetic resonance spectrum of liquid milk was examined. Of the three peaks observed, the two larger were assigned to inorganic phosphate (Pi) and the seryl phosphate (SerP) residues of casein; the third peak was assigned to a phosphodiester, which is probably glycerophosphoryl choline. The pH-dependences of the chemical shifts of the Pi and SerP were measured with and without added EDTA, and the results confirm the assignments. The width of the Pi peak in milk is significantly greater than in similar solutions lacking casein, probably because of binding to, or chemical exchange with, the casein micelle. Most of the SerP residues in milk are not sufficiently mobile to have been detected in these experiments but a significant fraction of SerP residues is able to move freely and can be titrated.

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