Earlier work from this group has suggested that, in electron capture and electron-transfer mass spectrometry experiments on positively charged gas-phase samples of polypeptides, the initial electron attachment event most likely occurs at one of the peptide's positively charged sites (e.g., protonated side chains), although electron attachment can occur at a disulfide or amide site ca. 1-10% of the time. Focusing on the 90-99% dominant channel in which initial electron attachment occurs at. a positive site, this paper addresses to what extent. and over what distances electron transfer can take place from a positively charged site to a disulfide sigma* or amide pi* orbital, because it is thought that it is through such orbitals that disulfide or N-C-alpha backbone bond cleavage occurs. Ab initio electronic structure calculations show that, as long as an SS sigma* (or OCN pi*) orbital experiences Sufficient Coulomb stabilization from proximal positively charged groups, there are a myriad of excited Rydberg states located oil positive sites that are able to induce such intrapeptide electron transfer. Computational data show that the transfer rates decay exponentially with distance fora given Rydberg orbital. An analytical model is developed that allows us to estimate the rates of Rydberg-to-valence and Rydberg-to-Rydberg electron transfers as functions of the Rydberg orbitals' it quantum numbers. This model suggests that transfer can occur over very long distances at rates that are more than competitive with the rates of radiationless relaxation within the manifold of Rydberg states (the latter processes eventually terminate the electron-transfer process an thus the disulfide or N-C-alpha bond cleavages), and it gives formulas for how these rates depend on n (and thus the radial span of the Rydberg orbitals),