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Protein in water solution increases magnetic relaxation rates of solvent nuclei to an extent that depends on magnetic field strength and molecular weight. Koenig and Schillinger (J. Biol. Chem. 244, 3283 (1969)) showed that a small fraction of the water molecules in the first hydration shell, bound irrotationally with a residence lifetime in the range 0.1(More)
The magnetic field dependence of the longitudinal relaxation rates 1/T1 (NMRD profiles) of blood and plasma from rabbits before and after injection of Gd(DTPA) are reported as a function of magnetic field strength from 0.01 to 50 MHz. Over 100 values along the time-dependent magnetization were recorded for each 1/T1 and analyzed for multiple exponentials.(More)
The bcl-2 family of proteins play an important role in the control of apoptosis. Family members exist which are either pro- or anti-apoptotic and their activity appears to control a checkpoint between signals from the cell surface and activation of the ICE-family of proteases. Despite having a key role to play in apoptosis, the mechanism of action of these(More)
The remarkable success of magnetic resonance imaging of adult brain relates to the unusually large ratio of the longitudinal relaxation rates 1/T1 of white and gray matter, approximately 2:1 at physiological temperature and traditional imaging fields. Several investigators have conjectured that myelin is the source of the greater 1/T1 of white matter(More)
CTED acknowledges the tremendous energy, thoughtful participation, and cooperation from members of the Advisory Committee. Special thanks to Rob Greenwood and Roma Call for their facilitation, patience, and perseverance keeping the Committee focused and moving forward. Overview Greenhouse gas emission reduction targets are established in Washington State(More)
We report results for proton 1/T1, 1/T2, and K, the rate of magnetization transfer from solvent to solute, for 5 and 10 wt. % solutions of bovine serum albumin, both native and chemically cross-linked, in undeuterated and approximately 50% deuterated water, at 4.7 T (200.1 MHz) and 19 degrees C. At this field, although K > 1/T1 for the cross-linked samples,(More)
It is well established that the longitudinal magnetic relaxation rate of solvent water protons, 1/T1, increases markedly in homogeneous protein solutions as the magnetic field is reduced well below the traditional NMR range. For a 5% solution of protein of 10(5) Da, for example, 1/T1 increases from about 50% above the pure water rate of 20 MHz to five times(More)
The magnetic field dependence of 1/T1 over the range 0.01 to 50 MHz proton Larmor frequency (NMRD profile) is reported for water protons in solutions of horse spleen apoferritin, and of ferritin reconstituted at both low and high iron levels. The apoferritin results are in every way typical of diamagnetic spherical proteins of their size (K. Hallenga and S.(More)
The magnetic field dependence of the solvent water proton longitudinal relaxation rate 1/T1 (the NMRD profile) has been measured for solutions of chelates of Gd3+ and Mn2+ ions with two different polyaza macrocyclic ligands: 1,4,7-triazacyclononane-N,N',N",-triacetic acid (NOTA) and 1,4,7,10-tetraazacyclododecane-N,N',N",N'"-tetraacetic acid (DOTA). Studies(More)