Oxidised lipids are reported to interact with proteins causing undesirable changes in nutritional and functional properties including a loss of amino acids, cross-linking and damage to proteins and DNA. ESR spectroscopy with spin trapping was used to study the type of radical species generated in methyl linoleate and the transfer of the radical to protein beta-lactoglobulin. Antioxidants vitamins C and E reduced lipid oxidation and subsequent transfer of the radical to the protein as shown by the shape and size of the radical adduct. Changes to protein molecular structure due to oxidation were investigated by multidimensional NMR spectroscopy and liquid chromatography. NMR spectra indicated that as a result of oxidation and protein denaturation, there was an increase in structural flexibility and some initially protected backbone amide groups were exposed as they become sharper and easily identifiable. Dityrosine was detected in all samples tested which is indicative of oxidative damage to proteins. Monitoring tyrosyl radicals and formation of dityrosine is of practical value in order to enhance the acceptability, nutritional and safety aspects of proteins.