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Proceedings Paper

Peptide sequencing using MALDI on time-of-flight and ion trap mass spectrometers
Author(s): Robert J. Cotter; Timothy J. Cornish; Marcela Cordero; Vladimir M. Doroshenko
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Paper Abstract

Two instruments have been developed in our laboratory for the direct amino-acid sequencing of peptides. The first is a time-of-flight (TOF) mass spectrometer that utilizes a coaxial, curved-field reflectron which provides simultaneous focusing of product ins formed by post- source decay (PSD) and obviates the need for scanning or stepping the reflectron voltage. The second is a matrix-assisted laser desorption/ionization (MALDI) ion trap mass spectrometer (ITMS). In this instrument, MALDI ions are trapped efficiently by ramping the trapping rf field, and a linear mass scale is achieved by modulating the axial excitation voltage during mass scanning. Monoisotopic mass selection and excitation is accomplished using phase- modulated SWIFT (stored waveform inverse Fourier transform) techniques, while efficient CID (collision-induced dissociation) performance is achieved using pulsed introduction of Xe and other heavier gases. Both mass spectrometers have been designed as compact instruments for sequencing peptides in partially fractionated mixtures.

Paper Details

Date Published: 1 April 1996
PDF: 12 pages
Proc. SPIE 2680, Ultrasensitive Biochemical Diagnostics, (1 April 1996); doi: 10.1117/12.237625
Show Author Affiliations
Robert J. Cotter, Johns Hopkins Univ. School of Medicine (United States)
Timothy J. Cornish, Johns Hopkins Univ. School of Medicine (United States)
Marcela Cordero, Johns Hopkins Univ. School of Medicine (United States)
Vladimir M. Doroshenko, Johns Hopkins Univ. School of Medicine (United States)


Published in SPIE Proceedings Vol. 2680:
Ultrasensitive Biochemical Diagnostics
Gerald E. Cohn; Steven A. Soper; C. H. Winston Chen, Editor(s)

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