Proton magnetic relaxation dispersion in aqueous biopolymer systems

Investigation of the magnetic field dependence of proton spin-lattice relaxation in solutions of bovine fibrinogen has been performed for Larmor frequencies between 50 Hz and 60 MHz, and complemented with measurements of spin-spin relaxation rates at 2 kHz and 25 MHz. A thorough analysis of experimental data, including the effects of protein concentration, temperature, pH and isotopic dilution, leads to an overall relaxation scheme consistent with T 1 and T 2 values at both low and high magnetic fields. The scheme involves water molecules slightly anisotropically bound on proteins as well as slow exchanging protein protons magnetically coupled to solute nuclei. A coherent picture, reminiscent of the traditional hydration layer, can be obtained for bound water. A major conclusion is that transfer of single protons may contribute substantially to the chemical exchange between free and bound water.