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	Spektroskopia ATR-FTIR	Dichroizm kołowy	Rezonans Powierzchniowy
Dziedzina	Spektroskopia	Spektroskopia	Spektroskopia
Rodzina	Process / pipeline	Process / pipeline	Process / pipeline
Rok powstania	1961	1969	1971
Twórca	Joop Fahrenfort	Jean-Claude Fasman	Erich Kretschmann
Typ	Vibrational spectroscopy technique	Spectroscopic method	Optical technique
Źródło pierwotne	Harrick, N. J. (1960). Study of physics of internal reflection from metals. Journal of Physics and Chemistry of Solids, 13(2), 143-155.	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.
Inne nazwy	ATR-IR, attenuated total reflectance, FTIR spectroscopy	CD spectroscopy, circular dichroism, CD analysis	SPR, surface plasmon, SPR biosensing
Pokrewne	3	3	3
Podsumowanie	Attenuated Total Reflectance (ATR) Fourier Transform Infrared (FTIR) spectroscopy is a variant of conventional FTIR that measures infrared absorption through evanescent-wave interrogation of samples in direct contact with a high-refractive-index crystal. Developed by Harrick and Fahrenfort in the 1960s, ATR-FTIR is now the dominant form of FTIR spectroscopy, enabling rapid, non-destructive characterization of organic compounds, polymers, coatings, and biological materials without extensive sample preparation.	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.