ABSTRACT
A method is described to synchronize the scans of the first and second double-focusing mass spectrometers of a tandem double-focusing mass spectrometer. The scans are synchronized by scanning the first mass spectrometer with voltages instead of the magnetic field. The method is demonstrated with scans that provide all of the precursor ions that produce a selected product ion (precursor ion scan). These precursor ion scans are compared to the previous method of obtaining precursor ion scans on a tandem double-focusing mass spectrometer. The precursor ion scans using the synchronized scanning allow for the use of high-energy collisions on any tandem double-focusing mass spectrometer, while limiting the mass range possible in a single scan. The limited mass range may be corrected by obtaining several spectra with different magnetic fields on the first mass spectrometer.
Subject(s)
Mass Spectrometry/methodsABSTRACT
The occurrence of charge-separation reactions in tandem mass spectrometry of doubly protonated angiotensin II is demonstrated by the use of mass-analyzed ion kinetic energy spectrometry (MIKES) and kinetic energy release distributions (KERDs). Linked scans at a constant B/E severely discriminate against product ions formed by charge-separation reactions. Although the products are significantly more abundant in MIKES experiments, instrumental discrimination still makes quantitation of relative product ion abundances highly inaccurate. The most probable KERs (T m. p.) and the average KERs (T ave.) of the reactions are determined from the KERDs, and these values are compared to the KERs determined from the peak widths at half-height (T 0. 5). The measurement of T 0. 5 is a poor approximation to T m. p. and T ave.. The T m. p. is used to calculate a most probable intercharge distance, which is compared to results from molecular dynamics calculations. The results provide evidence with regard to the mechanisms of fragmentation of multiply charged ions and the location of the charge site in relation to the decomposition reactions.
ABSTRACT
Scans of the electrostatic analyzer (ESA) across the precursor ion beam in reverse-geometry (BE) mass spectrometers that are operated under double-focusing conditions do not measure the "energy resolution of the main beam": They only measure double-focusing resolution. The only way that ESA scans can measure the kinetic energy distribution of the main beam is to operate the instrument so that angular (directional) focusing is not achieved. Thus, the mass spectrometer is no longer double-focusing. Under double-focusing conditions, however, scans of the accelerating voltage while the magnetic field and ESA are held constant can be used to measure either the kinetic energy distribution of the main beam that enters the magnet or the energy-resolving power of the instrument. Scans at a constant ratio of B(2)/E can be used similarly. The energy-resolving power of any ESA is defined by its dispersion and the widths of the energy-resolving object and image slits that immediately precede and follow the ESA, respectively. The use of BE, EB, and triple-sector instruments to measure energy-resolving power and the kinetic energy distribution of the precursor ion main beam is compared and discussed.
ABSTRACT
This article describes results of low-level (sub-femtomole) detection of peptides by matrix-assisted laser desorption ionization. The matrix-assisted laser desorption ionization method can be used for low-level detection of the parent ion, either [M + H](+) or [M + Na](+), and collision-induced dissociation of the parent ion can be performed at the picomole level. The instrument used for these studies is a novel high-performance magnetic sector (electric(E)/magnetic(B) sector)/reflectron time-of-flight (TOP) tandem mass spectrometer (EB/TOF).