Σύγκριση μεθόδων

	Συντονισμός Επιφανειακών Πλασμονίων	Διχρωισμός Κυκλικής Διάθλασης
Πεδίο	Φασματοσκοπία	Φασματοσκοπία
Οικογένεια	Process / pipeline	Process / pipeline
Έτος προέλευσης	1971	1969
Δημιουργός	Erich Kretschmann	Jean-Claude Fasman
Τύπος	Optical technique	Spectroscopic method
Θεμελιώδης πηγή	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.
Εναλλακτικές ονομασίες	SPR, surface plasmon, SPR biosensing	CD spectroscopy, circular dichroism, CD analysis
Συναφείς	3	3
Σύνοψη	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.	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.