The electron paramagnetic resonance (EPR) spectral features of several plasma-irradiated fibrous polypeptides (scleroproteins), such as silk, wool, and collagen vary with materials, but remain unchanged during the course of plasma irradiation in each case. Unlike for many other synthetic and natural homopolymers, it is difficult to identify the full structures of polypeptide radicals from EPR spectroscopic evidence alone, since proteins consist of many kinds of amino acid units. Nevertheless, systematic computer simulations indicated that plasma susceptibility for radical formation is rather specific in amino acids, that is glycine-derived, radicals (-CHNHCO-) in silk and collagen, and sulphide radicals (-RS) in wool as a major radical.