Compara mètodes

	MALDI-TOF	Dispersió de raigs X a petit angle (SAXS)	Reconeixement de Plasmons Superficials
Camp	Espectroscòpia	Espectroscòpia	Espectroscòpia
Família	Process / pipeline	Process / pipeline	Process / pipeline
Any d'origen	1988	1954	1971
Autor original	Michael Karas	Otto Kratky	Erich Kretschmann
Tipus	Ionization and mass analysis technique	Synchrotron/X-ray technique	Optical technique
Font seminal	Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.	Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
Àlies	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	SAXS, small-angle scattering	SPR, surface plasmon, SPR biosensing
Relacionats	3	3	3
Resum	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.	Small-Angle X-ray Scattering (SAXS) is a solution-phase X-ray scattering technique that measures the overall shape and size of macromolecules and nanoparticles by analyzing scattering intensity at low angles (0.1-10 degrees). Developed by Kratky and colleagues in the 1950s, SAXS provides information about molecular radius, aggregation state, and overall shape without requiring crystallization or fixing, making it ideal for studying native protein conformations and dynamics.	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.