Surface Induced Dissociation of Peptides using FTICR Mass Spectrometry
EMSL Project ID
3390
Abstract
This work will utilize the unique EMSL 6T FT-ICR mass spectrometer specially configured for SID studies to explore the fragmentation behavior of peptides and small proteins. Ion-surface impact is a fast and efficient means for excitation of ions of any size, for which deposition of energy into vibrational modes of the projectile molecule occurs on a timescale of picoseconds. Coupling SID with FT-ICR MS provides the distinct advantages of long and variable reaction times (milliseconds to seconds), which greatly reduces the kinetic shift and allows us to access the lowest-energy dissociation pathways for large molecules. Peptides and small proteins that will be examined in our FT-ICR SID studies have a large number of vibrational degrees of freedom (200-600), which results in a slow dissociation that is ideally suited for kinetic studies on a time scale of the FT-ICR mass spectrometer.Time- and collision energy resolved studies that can be conducted using the EMSL mass spectrometer provide very detailed information on the dissociation behavior of large ions. This will allow us to elucidate mechanisms of fragmentation of these species and develop fragmentation rules that are critical for improved identification of peptides and proteins and development of smart databases for proteomics research.
Project Details
Start Date
2003-03-15
End Date
2006-03-19
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members
Related Publications
Fernandez FM, VH Wysocki, JH Futrell, and J Laskin. 2006. "Protein Identification Via Surface-Induced Dissociation in an FT-ICR Mass Spectrometer and a Patchwork Sequencing Approach." Journal of the American Society for Mass Spectrometry 17(5):700-709.
Hess BM, J Xue, LM Markillie, RC Taylor, HS Wiley, BK Ahring, and BE Linggi. 2013. "Coregulation of terpenoid pathway genes and prediction of isoprene production in Bacillus subtilis using transcriptomics." PLoS One 8(6):e66104.