In this study, we used collision-induced dissociation (CID) to examine the gas-phase fragmentations of [G(n)W](center dot+) (n = 2-4) and [GXW](center dot+) (X = C, S, L, F, Y, Q) species. The C-beta-C-gamma bond cleavage of a C-terminal decarboxylated tryptophan residue ([M - CO2](center dot+)) can generate [M - CO2 - 116](+), [M - CO2 - 117](center dot+), and [1H-indole](center dot+) (m/z 117) species as possible product ions. Competition between the formation of [M - CO2 - 116](+) and [1H-indole](center dot+) systems implies the existence of a proton-bound dimer formed between the indole ring and peptide backbone. Formation of such a proton-bound dimer is facile via a protonation of the tryptophan gamma-carbon atom as suggested by density functional theory (DFT) calculations. DFT calculations also suggested the initially formed ion 2, the decarboxylated species that is active against C-beta-C-gamma. bond cleavage, can efficiently isomerize to form a more stable pi-radical isomer (ion 9) as supported by Rice-Ramsperger-Kassel-Marcus (RRKM) modeling. The C-beta-C-gamma bond cleavage of a tryptophan residue also can occur directly from peptide radical cations containing a basic residue. CID of [WG(n)R](center dot+) (n = 1-3) radical cations consistently resulted in predominant formation of [M - 116](+) product ions. It appears that the basic arginine residue tightly sequesters the proton and allows the charge-remote C-beta-C-gamma bond cleavage to prevail over the charge-directed one. DFT calculations predicted that the barrier for the former is 6.2 kcal mol(-1) lower than that of the latter. Furthermore, the pathway involving a salt-bridge intermediate also was accessible during such a bond cleavage event.