Cross relaxation and spin diffusion in the proton NMR of hydrated collagen

Abstract

PROTON NMR of water is being used extensively to probe the molecular dynamics of water molecules in biological systems such as protein solutions, hydrated macromolecules, cells and tissue. The nuclear magnetic relaxation rates R₁ (spin–lattice) and R₂ (spin–spin) can be analysed in terms of the rotational motions of the water molecules^1–3. A crucial assumption in this analysis is that the proton relaxation of the water proceeds independently of that of the macromolecules. Kimmich and Noack^4–6 claim that this assumption may be incorrect for proton spin–lattice relaxation because of spin diffusion, but clear evidence of spin diffusion in hydrated biological samples has not been reported. We show here that the proton spin–lattice relaxation behaviour in hydrated collagen is dominated by cross relaxation between the water protons and the macromolecular protons as a result of spin diffusion; the macromolecular spin–lattice relaxation contributes significantly to the water proton R₁.