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Energetics and Dynamics of Peptide Fragmentation from Multiple-Collision Activation and Surface-Induced Dissociation Studies

Journal Article · · European Journal of Mass Spectrometry, 10(2):259-267
DOI:https://doi.org/10.1255/ejms.641· OSTI ID:15007487
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 MS/MS data obtained using collisional activation. We demonstrate that surface-induced dissociation (SID) on a long timescale of Fourier transform ion cyclotron resonance mass spectrometer (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.
Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC06-76RL01830
OSTI ID:
15007487
Report Number(s):
PNNL-SA-39098; 6291; KC0302020
Journal Information:
European Journal of Mass Spectrometry, 10(2):259-267, Journal Name: European Journal of Mass Spectrometry, 10(2):259-267
Country of Publication:
United States
Language:
English

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