Photochemical reactions of free and N-acetyl alpha-amino acids with chlorine and deuterium labeled hydrogen peroxide have been used to determine both the relative rates of reaction of molecules of these classes and the relative reactivity of their different types of hydrogen toward abstraction by chlorine and oxygen centered radicals. The relative rates of reaction of these species range over more than 3 orders of magnitude; however, where data are available from more than one amino acid for a particular type of group at a specific position on the side chain, the values are remarkably similar. The predictive utility of these results has been demonstrated for the regioselective chlorination of tripeptides. More generally this analysis shows that the backbone and adjacent side chain positions of amino acids and peptides are peculiarly resistant to hydrogen atom transfer, and a similar pattern of reactivity has been noted from earlier studies of reactions of modified substrates catalyzed by isopenicillin-N-synthetase. Such resistance stands out in contrast to the common occurrence of free radical reactions of a-amino acids, peptides, and proteins and their importance in biology. Nevertheless, it provides a reason for the ability of amino acids and their derivatives to avoid degradation in Nature where they are constantly exposed to radicals, and it accounts, at least in part, for the anomalous ability of enzymes to catalyze free radical reactions without being broken down by the radical intermediates.