Módszerek összehasonlítása

	SERS	Körkörös dikroizmus	Felületi plazmon rezonancia
Tudományterület	Spektroszkópia	Spektroszkópia	Spektroszkópia
Módszercsalád	Process / pipeline	Process / pipeline	Process / pipeline
Keletkezés éve	1974	1969	1971
Megalkotó	Martin Fleischmann	Jean-Claude Fasman	Erich Kretschmann
Típus	Vibrational spectroscopy technique	Spectroscopic method	Optical technique
Alapmű	Fleischmann, M., Hendra, P. J., & McQuillan, A. J. (1974). Raman spectra of pyridine adsorbed at a silver electrode. Chemical Physics Letters, 26(2), 163-166.	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
Alternatív nevek	Surface-enhanced Raman scattering, SERS spectroscopy	CD spectroscopy, circular dichroism, CD analysis	SPR, surface plasmon, SPR biosensing
Kapcsolódó	3	3	3
Összefoglaló	Surface-Enhanced Raman Spectroscopy (SERS) amplifies weak Raman signals by many orders of magnitude when analyte molecules are adsorbed on specially prepared metal (typically silver or gold) nanostructured surfaces. Discovered by Fleischmann, Hendra, and McQuillan in 1974, SERS enables detection of vibrational signatures of single molecules and ultra-trace contaminants, revolutionizing analytical chemistry and forensics.	Circular Dichroism (CD) spectroscopy measures the differential absorption of left- and right-circularly polarized light by optically active molecules, particularly proteins and nucleic acids. Introduced by Greenfield and Fasman in 1969, CD is a rapid, non-destructive technique for characterizing secondary structure (alpha-helix, beta-sheet), monitoring protein folding transitions, and assessing conformational changes in response to pH, temperature, or ligand binding.	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.