Conventionally, electron capture or transfer to a polyprotonated peptide ion produces an initial radical-cation intermediate which dissociates "directly" to generate complementary c(n)' and z(m)(center dot) sequence ions (or ions and neutrals). Alternatively, or in addition, the initial radical-cation intermediate can undergo H-center dot migration to produce c(n)(center dot) (or c(n) - H-center dot) and z(m)' (or z(m)(center dot) + H-center dot) species prior to complex separation ("nondirect"). This reaction significantly complicates spectral interpretation, creates ambiguity in peak assignment, impairs effective algorithmic processing (reduction of the spectrum to solely C-12 m/z values), and reduces sequence ion signal-to-noise. Experimental evidence indicates that the products of hydrogen atom transfer reactions are substantially less prevalent for higher charge state precursors. This effect is generally rationalized on the basis of decreased complex lifetime. Here, we present a theoretical study of these reactions in post N-C-alpha bond cleavage radical-cation complexes as a function of size and precursor charge state. This approach provides a computational estimate of the barriers associated with these processes for highly charged peptides with little charge solvation. The data indicate that the H-center dot migration is an exothermic process and that the barrier governing this reaction rises steeply with precursor ion charge state. There is also some evidence for immediate product separation following N-C-alpha bond cleavage at higher charge state.