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| Dichroïsme circulaire× | MALDI-TOF× | |
|---|---|---|
| Domaine | Spectroscopie | Spectroscopie |
| Famille | Process / pipeline | Process / pipeline |
| Année d'origine≠ | 1969 | 1988 |
| Auteur d'origine≠ | Jean-Claude Fasman | Michael Karas |
| Type≠ | Spectroscopic method | Ionization and mass analysis technique |
| Source fondatrice≠ | Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116. DOI ↗ | Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301. DOI ↗ |
| Alias | CD spectroscopy, circular dichroism, CD analysis | MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry |
| 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. | Matrix-Assisted Laser Desorption/Ionization (MALDI) combined with Time-of-Flight (TOF) mass analysis, or MALDI-TOF, is a soft ionization mass spectrometry technique that gently ionizes intact biomolecules and volatile organic compounds, then measures their mass-to-charge ratio by measuring flight time through a field-free drift region. Introduced independently by Karas, Hillenkamp, and Tanaka in 1988, MALDI-TOF revolutionized proteomics, microbiology, and organic analysis by enabling mass determination of proteins and polymers exceeding 100 kDa. |
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