Water proton relaxation times, T1 and T2, were measured to assess the kinetics of the oxidative processes in biological samples. The oxidation in aqueous solutions of albumins was promoted by an addition of 3% hydrogen peroxide (H2O2). Immediately following this addition a sharp exponential decrease of both relaxation times was observed. As we confirmed experimentally, the time course of relaxation depended on several essential factors like structure and the concentration of proteins and also the presence of antioxidants added to solution. In experiments with protein solutions containing a small amount of ascorbic acid, after reaching a minimum, relaxation time increased towards the initial (pre-addition H2O2) values. We conclude that this T1 and T2 recovery is a consequence of the presence of antioxidants and may be used to evaluate its action. This study demonstrates that nuclear magnetic resonance (NMR) relaxation measurements may be useful in evaluating free radicals reactions and antioxidants capacity.

NMR relaxation provides powerful tools for obtaining information on three-dimensional structures, dynamic properties and intermolecular interactions of biological macromolecules. One of these methods, called dispersion profile, is based on measuring the field dependence of spin-relaxation rates in the rotating frame, R1ρ = 1/T1ρ, in the presence of a low magnetic field B1. In the presented study we use this method for investigation of molecular dynamics in protein samples. Dispersion profiles can be predicted theoretically and using two models, assuming either dipolar interaction between protons or power law dispersion, we have evaluated some molecular dynamic parameters of water adsorbed on protein surface. Our researches are focused on the connections of obtained parameters of molecular dynamics with conformation changes of protein. We have calculated the correlation times and power parameters for samples of lyophilized powder of albumins (egg white and bovine and rabbit blood serum) and lysozyme, as well as its aqueous solutions. Analysis of these parameters yields valuable information on the molecular nature of investigated biological systems. We also used this method to analyze experimental data of T1ρ obtained by other authors for bovine serum albumin and we have found good accordance with their conclusions concerning molecular dynamics of proteins.