Food and feed proteins are subject to oxidation reactions during production, processing, and storage. Several individual oxidized amino acids have been described in model systems and food; however, protein oxidation in food is still mostly assessed by the analysis of protein carbonylation. In the present review, the chemistry of protein oxidation and its implications for protein functionality, food flavor, and nutritional physiology are briefly summarized. Limitations of generic methods targeting redox-relevant functional groups and properties of typical reaction products, such as the determination of protein carbonyls and fluorescence spectroscopy, are presented. Methods for the quantitation of individual oxidation products of susceptible amino acids, such as cysteine, methionine, phenylalanine, tyrosine, and tryptophan, are reported. Special regard is paid to limitations resulting from the required hydrolysis procedures and unintended formation of the analytes during sample pretreatment. If available, results from food analysis obtained by different methods are compared. Suggestions and requirements for future works on protein oxidation in food and nutrition are given.