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| MALDI-TOF× | Körkörös dikroizmus× | Fourier Transzformáció-Ion Ciklotron Rezonancia (FT-ICR) tömegspektrometria× | |
|---|---|---|---|
| Tudományterület | Spektroszkópia | Spektroszkópia | Spektroszkópia |
| Módszercsalád | Process / pipeline | Process / pipeline | Process / pipeline |
| Keletkezés éve≠ | 1988 | 1969 | 1974 |
| Megalkotó≠ | Michael Karas | Jean-Claude Fasman | Alan Marshall |
| Típus≠ | Ionization and mass analysis technique | Spectroscopic method | Mass spectrometry technique |
| Alapmű≠ | Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301. DOI ↗ | 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 ↗ |
| Alternatív nevek | MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry | CD spectroscopy, circular dichroism, CD analysis | FT-ICR-MS, Fourier Transform ICR, ICR mass spectrometry |
| Kapcsolódó≠ | 3 | 3 | 4 |
| Összefoglaló≠ | 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. | 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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