This account summarizes the energetics and dynamics of peptide fragmentation obtained using a new approach recently developed in our laboratory. The approach involves RRKM modeling of time- and energy- resolved tandem mass spectrometry (MS/MS) data obtained using collisional activation. We demonstrate that surface-induced dissociation (SID) on a long time-scale of Fourier transform ion cyclotron resonance mass spectrometry (FT-ICR MS) is perfectly suited for studying the energetics and dynamics of peptide fragmentation. The advantages provided by SID include very fast ion activation, which eliminates possible discrimination against higher-energy dissociation pathways, and efficient "amplification" of small changes in dissociation parameters. We present a summary of results obtained for small alanine-containing peptides as well as larger peptides including angiotensin analogs and a series of peptides containing the LDIFSDF motif.