Comparer des méthodes

	Dichroïsme circulaire	Diffusion des rayons X aux petits angles (SAXS)	Résonance des Plasmons de Surface
Domaine	Spectroscopie	Spectroscopie	Spectroscopie
Famille	Process / pipeline	Process / pipeline	Process / pipeline
Année d'origine	1969	1954	1971
Auteur d'origine	Jean-Claude Fasman	Otto Kratky	Erich Kretschmann
Type	Spectroscopic method	Synchrotron/X-ray 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.	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.
Alias	CD spectroscopy, circular dichroism, CD analysis	SAXS, small-angle scattering	SPR, surface plasmon, SPR biosensing
Apparentées	3	3	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.	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.