The radical cationic reactivity of the peptide analogue molecule CH3CO-Gly-NH2 is addressed both experimentally and theoretically. The radical cation intermediate of CH3CO-Gly-NH2 is created by single-photon ionization of this molecule at 118.22 rim (similar to 10.5 eV). The two most stable conformers (C-7 and C-5) of this molecule exhibit different folds along the backbone: the C-7 conformer has a gamma-tum structure, and the C-5 conformer has a beta-strand structure. The experimental results show that the radical cation intermediate of CH3CO-Gly-NH2 dissociates and generates a fragment-ion signal at 73 amu that is observed through TOFMS. Theoretical results show how the fragment-ion signal at 73 amu is generated by only one conformer of CH3CO-Gly-NH2 (C-7) and how local charge and specific hydrogen bonding in the molecule influence fragmentation of the radical cation intermediate of CH3CO-Gly-NH2. The specific fold of the molecule controls fragmentation of this reactive radical cation intermediate. Whereas the radical cation of the C-7 conformer dissociates through a hydrogen-transfer mechanism followed by HNCO elimination, the radical cation of the C-5 conformer does not dissociate at all. CASSCF calculations show that positive charge in the radical cationic C-7 conformer is localized at the NH2CO moiety of the molecular ion. This site-specific localization of the positive charge enhances the acidity of the terminal NH2 group, facilitating hydrogen transfer from the NH2 to the COCH3 end of the molecular ion. Positive charge in the C-5 conformer of the CH3CO-Gly-NH2 radical cation is, however, localized at the COCH3 end of the molecular ion, and this conformer does not have enough energy to surmount the energy barrier to dissociation on the ion potential energy surface. CASSCF results show that conformation-specific localization of charge in the CH3CO-Gly-NH2 molecular ion occurs as a result of the different hydrogen-bonding interactions involved in the different molecular conformers.