مقایسهٔ روش‌ها

	ولتانومتری چرخه‌ای	رودی-کوتِکی-لوویچ	رزونانس پلاسمون سطحی
حوزه	طیف‌سنجی	طیف‌سنجی	طیف‌سنجی
خانواده	Process / pipeline	Process / pipeline	Process / pipeline
سال پیدایش	1964	1962	1971
پدیدآور	Randles Semyon Nicholson	Veniamin Levich	Erich Kretschmann
نوع	Electrochemical technique	Electrochemical technique	Optical technique
منبع بنیادین	Nicholson, R. S., & Shain, I. (1964). Electroanalytical chemistry. Analytical Chemistry, 36(4), 706-723.	Levich, V. G. (1962). Physicochemical Hydrodynamics. Prentice Hall.	Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324.
نام‌های دیگر	CV, cyclic voltammetry, electrochemistry	RDE, rotating disk electrode, Koutecky-Levich	SPR, surface plasmon, SPR biosensing
مرتبط	3	3	3
خلاصه	Cyclic Voltammetry (CV) is an electrochemical technique that measures redox reactions by varying the voltage applied to an electrode and monitoring the resulting current. Developed by Nicholson and Shain in 1964, CV is one of the most widely used electrochemical methods, providing rapid information about the redox potentials and electron-transfer kinetics of molecules and materials.	Rotating Disk Electrode (RDE) electrochemistry combined with Koutecky-Levich analysis is a powerful electrochemical technique that decouples diffusion-limited and kinetically limited electron-transfer processes. Developed by Levich in the 1960s, RDE enables determination of heterogeneous electron-transfer rate constants and mechanistic information by rotating an electrode to control mass transport.	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.