Abstract
Publisher Summary This chapter describes the theoretical considerations and experimental detail necessary for the implementation of the pulse-gradient spin-echo (PGSE) nuclear magnetic resonance (NMR) experiment for the study of translational motion. The investigation of proteins is emphasized, although measurements of water and metabolite molecular diffusion in biological systems will also be considered. PGSE NMR has been employed to study the concentration and temperature dependence of dilute aqueous protein solutions by observation of the proton signal at a static field strength of 0.40 T. Measurements of the self-diffusion coefficient for hemoglobin as a function of concentration by PGSE NMR spectroscopy compare favorably with those obtained by the use of other techniques. The measurement of protein diffusion in intact cells by PGSE NMR is feasible as demonstrated by the determination of the self-diffusion coefficients for oxyhemoglobin A and oxyhemoglobin S in the red blood cell. There have been numerous NMR studies of cellular and protein systems where water diffusion has been investigated. This chapter also describes the theoretical basis and application of magnetic field-gradient NMR techniques for the assessment of translational diffusion in a variety of systems.
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