Comparer des méthodes

	MALDI-TOF	Spectrométrie de masse par transformée de Fourier à cyclotron ionique (FT-ICR)
Domaine	Spectroscopie	Spectroscopie
Famille	Process / pipeline	Process / pipeline
Année d'origine	1988	1974
Auteur d'origine	Michael Karas	Alan Marshall
Type	Ionization and mass analysis technique	Mass spectrometry technique
Source fondatrice	Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.	Comisarow, M. B., & Marshall, A. G. (1974). Fourier transform ion cyclotron resonance spectroscopy. Chemical Physics Letters, 25(2), 282-283.
Alias	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry
Apparentées	3	4
Résumé	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.	Fourier 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.