2007
DOI: 10.1016/j.jmr.2007.02.006
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Relaxation of protons by radicals in rotationally immobilized proteins

Abstract: Proton spin-lattice relaxation by paramagnetic centers may be dramatically enhanced if the paramagnetic center is rotationally immobilized in the magnetic field. The details of the relaxation mechanism are different from those appropriate to solutions of paramagnetic relaxation agents. We report here large enhancements in the proton spin-lattice relaxation rate constants associated with organic radicals when the radical system is rigidly connected with a rotationally immobilized macromolecular matrix such as a… Show more

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Cited by 11 publications
(10 citation statements)
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“…The relaxivities of Gd 3+ -DTPA, Gd 3+ -DOTA-CAT, and Gd 3+ -DOTA-CAT (cleaved) , in 10% heat-treated BSA at pH 7 were measured at fields ranging from 0.24 mT to 9.4 T. Generally, relaxivity decreased as a function of field strengths similar to previous results (33). The NMRD profiles were similar to that shown for heat-treated BSA tissue phantoms and human brain tissues Figure 11.…”
Section: Discussionsupporting
confidence: 83%
“…The relaxivities of Gd 3+ -DTPA, Gd 3+ -DOTA-CAT, and Gd 3+ -DOTA-CAT (cleaved) , in 10% heat-treated BSA at pH 7 were measured at fields ranging from 0.24 mT to 9.4 T. Generally, relaxivity decreased as a function of field strengths similar to previous results (33). The NMRD profiles were similar to that shown for heat-treated BSA tissue phantoms and human brain tissues Figure 11.…”
Section: Discussionsupporting
confidence: 83%
“…[5]. For instance, proton spin-lattice relaxation induced by paramagnetic centers is dramatically enhanced for rotationally immobilized protein [37]. For these immobilized proteins rare binding sites for water in protein systems add very low frequency components to the dynamics spectrum.…”
Section: Introductionmentioning
confidence: 99%
“…Section 9 covers some applications of FFC NMR for probing the molecular dynamics in macromolecules and proteins. An application of FFC relaxometry is shown on water dynamics at the surface of various macromolecules and proteins [37,38]. Last, the application to NMRD in biological tissues of animals and in vivo MRI of human brains is briefly described [40].…”
Section: Introductionmentioning
confidence: 99%
“…However, for rotationally immobilized paramagnets rigidly bound to proteins, the magnetic field dependence of the 1 H spin‐lattice‐relaxation‐rate constant is similar to that in Eq. 2 at high magnetic field, that is, a power law in the Larmor frequency; the surface diffusive paramagnetic contributions will be described by a logarithmic dependence as well, but the scaling coefficient B will be larger (36, 37). Thus, in the high frequency regime, above the relaxation dispersion associated with free metals or protein‐bound metal ions (38), the form of Eq.…”
Section: Resultsmentioning
confidence: 99%