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| Dichroïsme circulaire× | Spectrométrie de masse par transformée de Fourier à cyclotron ionique (FT-ICR)× | |
|---|---|---|
| Domaine | Spectroscopie | Spectroscopie |
| Famille | Process / pipeline | Process / pipeline |
| Année d'origine≠ | 1969 | 1974 |
| Auteur d'origine≠ | Jean-Claude Fasman | Alan Marshall |
| Type≠ | Spectroscopic method | Mass spectrometry technique |
| Source fondatrice≠ | Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116. DOI ↗ | Comisarow, M. B., & Marshall, A. G. (1974). Fourier transform ion cyclotron resonance spectroscopy. Chemical Physics Letters, 25(2), 282-283. DOI ↗ |
| Alias | CD spectroscopy, circular dichroism, CD analysis | FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry |
| Apparentées≠ | 3 | 4 |
| 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. | Fourier Transform Ion Cyclotron Resonance (FT-ICR) mass spectrometry is an advanced analytical technique that combines magnetic confinement of ions with Fourier transform data processing to achieve exceptional mass accuracy and resolution. Developed by Comisarow and Marshall in 1974, FT-ICR-MS enables the determination of exact masses and elemental compositions of complex molecules, making it invaluable for environmental chemistry, metabolomics, petroleum characterization, and structural elucidation of unknowns. |
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