Electrospray ionization-mass spectrometry and tandem mass spectrometry
The ability to produce multiply charged molecular ions for biomolecules allows mass spectrometers to analyze compounds with molecular weights much in excess of the instrument's mass limit, but within the mass-to-charge range of most conventional mass spectrometers. In fact, proteins with molecular weights in excess of 130,000 daltons have been successfully analyzed by EIS-MS with a quadrupole mass spectrometer of limited m/z range (1700) in our laboratory. We have compared the ESI mass spectra of large proteins with and without reduction of its disulfide bridges. By cleavage of cysteine-cysteine bonds and thereby affecting the tertiary structure of the protein, a dramatic increase in the number of positive charges is observed. Highly charged ions desorbed from the droplets are sampled through a nozzle-skimmer orifice to be detected by the quadrupole mass spectrometer. Increasing collision energies also yields significant fragmentation of large peptide and proteins. 3 refs.
- Research Organization:
- Pacific Northwest Lab., Richland, WA (USA)
- DOE Contract Number:
- AC06-76RL01830
- OSTI ID:
- 5923916
- Report Number(s):
- PNL-SA-16621; CONF-8905166-1; ON: DE89014465
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
400201* -- Chemical & Physicochemical Properties
640304 -- Atomic
Molecular & Chemical Physics-- Collision Phenomena
74 ATOMIC AND MOLECULAR PHYSICS
CHARGED PARTICLES
COLLISIONS
DISSOCIATION
DROPLETS
IONIZATION
IONS
MASS SPECTROMETERS
MEASURING INSTRUMENTS
MOLECULAR STRUCTURE
MOLECULES
ORGANIC COMPOUNDS
PARTICLES
PROTEINS
SPECTROMETERS