Comparar métodos
Revisa los métodos seleccionados uno junto a otro; las filas que difieren aparecen resaltadas.
| Resonancia de Plasmones Superficiales× | Dicroísmo Circular× | |
|---|---|---|
| Campo | Espectroscopia | Espectroscopia |
| Familia | Process / pipeline | Process / pipeline |
| Año de origen≠ | 1971 | 1969 |
| Autor original≠ | Erich Kretschmann | Jean-Claude Fasman |
| Tipo≠ | Optical technique | Spectroscopic method |
| Fuente seminal≠ | 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 ↗ |
| Alias | SPR, surface plasmon, SPR biosensing | CD spectroscopy, circular dichroism, CD analysis |
| Relacionados | 3 | 3 |
| Resumen≠ | 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. |
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