31P Spin-Lattice Relaxation Times and Resonance Linewidths of Rat Tissuein Vivo: Dependence upon the Static Magnetic Field Strength

1985 ◽  
Vol 2 (4) ◽  
pp. 410-417 ◽  
Author(s):  
Jeffrey L. Evelhoch ◽  
Coleen S. Ewy ◽  
Barry A. Siegfried ◽  
Joseph J. H. Ackerman ◽  
David W. Rice ◽  
...  
Keyword(s):  
Magnetic Field ◽  
Field Strength ◽  
Magnetic Field Strength ◽  
Static Magnetic Field ◽  
Relaxation Times ◽  
Lattice Relaxation ◽  
Spin Lattice Relaxation ◽  
Spin Lattice

scholarly journals Effect of magnetic field strength on the linewidth and spin-lattice relaxation time of the thiocyanate carbon of cyanylated β-lactoglobulin B: optimization of the experimental parameters for observing thiocyanate carbons in proteins

1995 ◽  
Vol 306 (2) ◽  
pp. 531-535
Author(s):  
J P G Malthouse ◽  
P Phelan
Keyword(s):  
Magnetic Field ◽  
Field Strength ◽  
Magnetic Field Strength ◽  
Chemical Shift Anisotropy ◽  
Relaxation Times ◽  
Lattice Relaxation ◽  
Spin Lattice Relaxation ◽  
Spin Lattice Relaxation Time ◽  
Spin Lattice ◽  
Field Strengths

The linewidths and spin-lattice relaxation times of the 13C-n.m.r. signal at 109.7 p.p.m. due to the thiocyanate carbon of intact [cyanato-13C]cyanylated-beta-lactoglobulin-B have been determined at magnetic field strengths of 1.88, 6.34 and 11.74 T as well as the spin-lattice relaxation times of its backbone alpha-carbon atoms. The linewidths were directly proportional to the square of the magnetic field strength and we conclude that, at magnetic field strengths of 6.34 T or above, more than 70% of the linewidth will be determined by chemical-shift anisotropy. We estimate that the spin-lattice relaxation time resulting from the chemical-shift anisotropy of the thiocyanate carbon is 1.52 +/- 0.1 s and we conclude that for magnetic field strengths of 6.34 T and above the observed spin-lattice relaxation time of the thiocyanate carbon will be essentially independent of magnetic field strength. Using the rigid-rotor model we obtain estimates of the rotational correlation time of [cyanato-13C]cyanylated-beta-lactoglobulin-B and of the chemical-shift anisotropy shielding tensor of its thiocyanate carbon. We have calculated the linewidths and spin-lattice relaxation times of thiocyanate carbons at magnetic field strengths of 1.88-14.1 T in proteins with M(r) values in the range 10,000-400,000. The effects of magnetic field strength on the resolution and signal-to-noise ratios of the signals due to thiocyanate carbons attached to proteins of M(r) greater than 10,000 are discussed.

scholarly journals 19F spin–lattice relaxation of perfluoropolyethers: Dependence on temperature and magnetic field strength (7.0–14.1T)

2014 ◽  
Vol 242 ◽  
pp. 18-22 ◽  
Author(s):  
Deepak K. Kadayakkara ◽  
Krishnan Damodaran ◽  
T. Kevin Hitchens ◽  
Jeff W.M. Bulte ◽  
Eric T. Ahrens
Keyword(s):  
Magnetic Field ◽  
Field Strength ◽  
Magnetic Field Strength ◽  
Lattice Relaxation ◽  
Spin Lattice Relaxation ◽  
Spin Lattice

Nitrogen-14 quadrupole cross-relaxation spectroscopy

1988 ◽  
Vol 416 (1850) ◽  
pp. 149-178 ◽  
Keyword(s):  
Magnetic Field ◽  
Double Resonance ◽  
Relaxation Times ◽  
High Sensitivity ◽  
Lattice Relaxation ◽  
Cross Relaxation ◽  
Spin Lattice Relaxation ◽  
Proton Relaxation ◽  
Spin Lattice ◽  
Quadrupole Resonance

Cross-relaxation spectroscopy can be used as a sensitive method of detecting 14 N quadrupole-resonance signals in hydrogen-containing solids. The 1 H spin system is polarized in a high magnetic field that is then reduced adiabatically to a much lower value satisfying the level­-crossing condition, when the 1 H Zeeman splitting matches one of the 14 N quadrupole splittings. If the 14 N spin–lattice relaxation time is much shorter than that of the 1 H nuclei, a drastic loss of 1 H polarization occurs that is measured by recording the residual 1 H magnetic resonance signal after the sample has been returned to the higher field. The experimental cycle can be run in several different ways according to the relative values of the 1 H spin–lattice relaxation times ( T 1 ) in high and low field, the 14 N spin–lattice relaxation ( T 1Q ) and cross-polarization times ( T CP ), all of which can markedly influence the spectra. The line shapes are broadened by the presence of the magnetic field and Zeeman shifts of the peak frequencies also occur, for which simple corrections may be derived. The methods used have high sensitivity, particularly if the ratio T 1 / T 1Q is large. They have the advantage over other double-resonance techniques in that long proton T 1 values are not necessary for the success of an experiment; it is also possible to select conditions in which the recovered 1 H signal is directly proportional to the relative numbers of 14 N nuclei present and the magnitude of the cross-relaxation field. Multi-proton relaxation jumps also give rise to signals at subharmonics of the fundamental, whose relative intensities reflect the extent to which the 14 N and 1 H relaxation is coupled via their dipole–dipole interactions, which are not completely quenched in the finite magnetic fields necessary in cross-relaxation spectroscopy. These conclusions are illustrated in a number of 14 N spectra of compounds in which quadrupole-resonance signals have not previously been recorded.

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