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Relaxation time biological macromolecules

In small molecules, these artifacts are rarely observed because crossrelaxation rates are small. However, in biological macromolecules, crossrelaxation rates become competitive with the rate of Hartmann-Hahn transfer, because they increase with the correlation time or molecular weight. Fortunately, in large molecules it is possible to suppress contribitu-ions from cross-relaxation, based on the opposite signs of transverse and longitudinal cross-relaxation rates and (Griesinger et al.,... [Pg.173]

The other way that Cl NMR can be used in biological systems is in the study of chloride bound to proteins or other macromolecules. Sometimes this can be done by direct visualization of the resonance or from its free induction decay. More commonly it is performed by relaxation time measurements provided that there is rapid exchange of bound and free anions, because bound chloride relaxes very much more rapidly than free chloride. Frequently, double quantum filtered (DQF) spectra are employed which give useful information on chlorine bound to sites on the macromolecule. [Pg.680]

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