The effect of nitrogen-15 proton-driven spin diffusion on quantitative N-15 T-1 measurements in solid proteins is investigated, and the impact on the measurement of dynamic parameters is assessed. A simple model of exchange between neighboring nitrogens is used to reproduce the evolution of N-15 spin systems whose longitudinal relaxation rates and exchange rates are compatible with experimental measurements. We show that the induced error in the measured T-1 and its effect on the determination of dynamics parameters is likely to be less than the current experimental error. The use of deuterated protein samples is shown to have a small but sometimes visible effect, and may also considerably slow down or even suppress the exchange of magnetization due to spin diffusion. (c) 2006 Elsevier Inc. All rights reserved.