เปรียบเทียบวิธี

	การสั่นพ้องของพลาสมอนพื้นผิว	Circular Dichroism	แคลอริเมทรีแบบไทเทรตที่อุณหภูมิคงที่
สาขาวิชา	สเปกโทรสโกปี	สเปกโทรสโกปี	สเปกโทรสโกปี
ตระกูล	Process / pipeline	Process / pipeline	Process / pipeline
ปีกำเนิด	1971	1969	1989
ผู้ริเริ่ม	Erich Kretschmann	Jean-Claude Fasman	Terrence Wiseman
ประเภท	Optical technique	Spectroscopic method	Biophysical technique
แหล่งต้นตำรับ	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.	Wiseman, T., Williston, S., Brandts, J. F., & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry, 179(1), 131-137.
ชื่อเรียกอื่น	SPR, surface plasmon, SPR biosensing	CD spectroscopy, circular dichroism, CD analysis	ITC, isothermal calorimetry, microcalorimetry
ที่เกี่ยวข้อง	3	3	3
สรุป	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.	Isothermal Titration Calorimetry (ITC) is a thermodynamic technique that measures heat released or absorbed during biomolecular binding events at constant temperature. Developed by Wiseman and colleagues in 1989, ITC directly determines binding affinity (Kd), enthalpy (ΔH), and entropy (ΔS) in a single experiment, making it one of the most comprehensive methods for characterizing molecular interactions without requiring labels or immobilization.