Comparer des méthodes

	MALDI-TOF	Spectrométrie de masse par transformée de Fourier à cyclotron ionique (FT-ICR)	Résonance des Plasmons de Surface
Domaine	Spectroscopie	Spectroscopie	Spectroscopie
Famille	Process / pipeline	Process / pipeline	Process / pipeline
Année d'origine	1988	1974	1971
Auteur d'origine	Michael Karas	Alan Marshall	Erich Kretschmann
Type	Ionization and mass analysis technique	Mass spectrometry technique	Optical 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.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
Alias	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry	SPR, surface plasmon, SPR biosensing
Apparentées	3	4	3
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.	Surface Plasmon Resonance (SPR) is a real-time, label-free technique for detecting and monitoring biomolecular interactions at a sensor surface by measuring changes in the refractive index caused by ligand binding. Developed by Kretschmann in 1971 and applied to biosensing by Liedberg, Nylander, and Lundström in 1983, SPR is now a gold standard for measuring binding kinetics (association and dissociation rates) and equilibrium binding constants in protein interactions, antibody-antigen recognition, and drug discovery.