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FT-ICR Mass Spectrometry×MALDI-TOF×
OborSpektroskopieSpektroskopie
RodinaProcess / pipelineProcess / pipeline
Rok vzniku19741988
TvůrceAlan MarshallMichael Karas
TypMass spectrometry techniqueIonization and mass analysis technique
Původní zdrojComisarow, M. B., & Marshall, A. G. (1974). Fourier transform ion cyclotron resonance spectroscopy. Chemical Physics Letters, 25(2), 282-283. DOI ↗Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301. DOI ↗
Další názvyFT-ICR-MS, Fourier Transform ICR, ICR mass spectrometryMALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry
Příbuzné43
ShrnutíFourier Transform Ion Cyclotron Resonance (FT-ICR) mass spectrometry is an advanced analytical technique that combines magnetic confinement of ions with Fourier transform data processing to achieve exceptional mass accuracy and resolution. Developed by Comisarow and Marshall in 1974, FT-ICR-MS enables the determination of exact masses and elemental compositions of complex molecules, making it invaluable for environmental chemistry, metabolomics, petroleum characterization, and structural elucidation of unknowns.Matrix-Assisted Laser Desorption/Ionization (MALDI) combined with Time-of-Flight (TOF) mass analysis, or MALDI-TOF, is a soft ionization mass spectrometry technique that gently ionizes intact biomolecules and volatile organic compounds, then measures their mass-to-charge ratio by measuring flight time through a field-free drift region. Introduced independently by Karas, Hillenkamp, and Tanaka in 1988, MALDI-TOF revolutionized proteomics, microbiology, and organic analysis by enabling mass determination of proteins and polymers exceeding 100 kDa.
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ScholarGatePorovnat metody: FT-ICR Mass Spectrometry · MALDI-TOF. Získáno 2026-06-19 z https://scholargate.app/cs/compare