Surface-induced dissociation on a MALDI-ion mobility-orthogonal time-of-flight mass spectrometer: sequencing peptides from an "in-solution" protein digest. Academic Article uri icon

abstract

  • Peptide sequencing by surface-induced dissociation (SID) on a MALDI-ion mobility-orthogonal TOF mass spectrometer is demonstrated. SID of approximately 100-fmol amounts of model peptides HLGLAR (m/z 666.8), gramicidin S (m/z 1142.5), and bovine insulin b chain (m/z 3495.5) was accomplished using hydrocarbon-coated gold grids and approximately 20-eV collision energies. The current version of the instrument achieves a mobility resolution of approximately 20 and TOF mass resolution better than 200. Peptide sequences of four peptides from a tryptic digest of cytochrome c (approximately 1 pmol deposited) were obtained. The advantage of IM-SID-o-TOF-MS is that a single experiment can be used to simultaneously measure the molecular weights of the tryptic peptide fragments (e.g., peptide mass mapping) and partial sequence analysis, (e.g., real-time tandem mass spectrometry.)

published proceedings

  • Anal Chem

altmetric score

  • 3

author list (cited authors)

  • Stone, E., Gillig, K. J., Ruotolo, B., Fuhrer, K., Gonin, M., Schultz, A., & Russell, D. H.

citation count

  • 83

complete list of authors

  • Stone, E||Gillig, KJ||Ruotolo, B||Fuhrer, K||Gonin, M||Schultz, A||Russell, DH

publication date

  • May 2001