Σύγκριση μεθόδων

	Φασματομετρία Μάζας Μετασχηματισμού Fourier Κυκλοτρονίου Ιόντων (FT-ICR)	Συντονισμός Επιφανειακών Πλασμονίων
Πεδίο	Φασματοσκοπία	Φασματοσκοπία
Οικογένεια	Process / pipeline	Process / pipeline
Έτος προέλευσης	1974	1971
Δημιουργός	Alan Marshall	Erich Kretschmann
Τύπος	Mass spectrometry technique	Optical technique
Θεμελιώδης πηγή	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.
Εναλλακτικές ονομασίες	FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry	SPR, surface plasmon, SPR biosensing
Συναφείς	4	3
Σύνοψη	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.