Alteration of protein structure induced by low-energy (<18 eV) electrons. I. The peptide and disulfide bridges.

We present measurements of low-energy (<18 eV) electron-stimulated desorption of anions from acetamide (CH(3)CONH(2)) and dimethyl disulfide [DMDS: (CH(3)S)(2)] films. Electron irradiation of physisorbed CH(3)CONH(2) produces H(-), CH(3)(-) and O(-) anions, whereas the H(-), CH(2)(-), CH(3)(-), S(-), SH(-) and SCH(3)(-) anions are observed to desorb from the DMDS film. Below 12 eV, the dependence of the anion yields on the incident electron energy exhibits structures that indicate that a resonant process (i.e. dissociative electron attachment) is responsible for molecular fragmentation. Within the range of 1-18 eV, it is found that (1.7 and 1.4) x 10(7) H(-) ions/incident electron and (7.8 x 10(-11) and 4.3 x 10(-8)) of the other ions/incident electron are desorbed from acetamide and DMDS films, respectively. These results suggest that, within proteins, the disulfide bond is more sensitive to low-energy electron attack than the peptide bond. In biological cells, some proteins interact closely with nucleic acid. Therefore, the observed fragments, when produced from secondary low-energy electrons generated by high-energy radiation, not only may denature proteins, but may also induce reactions with the nearby nucleic acid and damage DNA.