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Dichroizm kołowy×Rezonans Powierzchniowy×
DziedzinaSpektroskopiaSpektroskopia
RodzinaProcess / pipelineProcess / pipeline
Rok powstania19691971
TwórcaJean-Claude FasmanErich Kretschmann
TypSpectroscopic methodOptical technique
Źródło pierwotneGreenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116. DOI ↗Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324. link ↗
Inne nazwyCD spectroscopy, circular dichroism, CD analysisSPR, surface plasmon, SPR biosensing
Pokrewne33
PodsumowanieCircular 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.
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ScholarGatePorównaj metody: Circular Dichroism · Surface Plasmon Resonance. Pobrano 2026-06-18 z https://scholargate.app/pl/compare