Energetics and dynamics of peptide fragmentation from multiple-collision activation and surface-induced dissociation studies.
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.
Laskin
Julia
J
Fundamental Science Directorate, Pacific Northwest National Laboratory, PO Box 999 (K8-88), Richland, WA 99352, USA. Julia.Laskin@pnl.gov
D000595:Amino Acid Sequence; D007700:Kinetics; D013058:Mass Spectrometry; D010455:Peptides / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
D010455:Peptides