Comparer des méthodes

	Dichroïsme circulaire	Spectrométrie de masse par transformée de Fourier à cyclotron ionique (FT-ICR)	Résonance des Plasmons de Surface
Domaine	Spectroscopie	Spectroscopie	Spectroscopie
Famille	Process / pipeline	Process / pipeline	Process / pipeline
Année d'origine	1969	1974	1971
Auteur d'origine	Jean-Claude Fasman	Alan Marshall	Erich Kretschmann
Type	Spectroscopic method	Mass spectrometry technique	Optical technique
Source fondatrice	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.	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.
Alias	CD spectroscopy, circular dichroism, CD analysis	FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry	SPR, surface plasmon, SPR biosensing
Apparentées	3	4	3
Résumé	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.	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.