方法对比
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| 表面等离激元共振× | 圆二色性× | 等温滴定量热法× | |
|---|---|---|---|
| 领域 | 光谱学 | 光谱学 | 光谱学 |
| 方法族 | Process / pipeline | Process / pipeline | Process / pipeline |
| 起源年份≠ | 1971 | 1969 | 1989 |
| 提出者≠ | Erich Kretschmann | Jean-Claude Fasman | Terrence Wiseman |
| 类型≠ | Optical technique | Spectroscopic method | Biophysical technique |
| 开创性文献≠ | Kretschmann, E. (1971). Determination of optical constants of metals by excitation of surface plasmons. Zeitschrift für Physik, 241(4), 313-324. link ↗ | Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116. DOI ↗ | 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. DOI ↗ |
| 别名 | SPR, surface plasmon, SPR biosensing | CD spectroscopy, circular dichroism, CD analysis | ITC, isothermal calorimetry, microcalorimetry |
| 相关 | 3 | 3 | 3 |
| 摘要≠ | 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. |
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