विधियों की तुलना करें

	MALDI-TOF	FT-ICR Mass Spectrometry	पृष्ठ प्लास्मोन अनुनाद
क्षेत्र	स्पेक्ट्रोस्कोपी	स्पेक्ट्रोस्कोपी	स्पेक्ट्रोस्कोपी
परिवार	Process / pipeline	Process / pipeline	Process / pipeline
उद्भव वर्ष	1988	1974	1971
प्रवर्तक	Michael Karas	Alan Marshall	Erich Kretschmann
प्रकार	Ionization and mass analysis technique	Mass spectrometry technique	Optical technique
मौलिक स्रोत	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.
उपनाम	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry	SPR, surface plasmon, SPR biosensing
संबंधित	3	4	3
सारांश	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.