Comparer des méthodes
Examinez les méthodes sélectionnées côte à côte ; les lignes qui diffèrent sont mises en évidence.
| Dichroïsme circulaire× | Calorimétrie par titration isotherme× | |
|---|---|---|
| Domaine | Spectroscopie | Spectroscopie |
| Famille | Process / pipeline | Process / pipeline |
| Année d'origine≠ | 1969 | 1989 |
| Auteur d'origine≠ | Jean-Claude Fasman | Terrence Wiseman |
| Type≠ | Spectroscopic method | Biophysical technique |
| Source fondatrice≠ | 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 ↗ |
| Alias | CD spectroscopy, circular dichroism, CD analysis | ITC, isothermal calorimetry, microcalorimetry |
| Apparentées | 3 | 3 |
| Résumé≠ | 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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