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| MALDI-TOF× | SAXS× | |
|---|---|---|
| Valdkond | Spektroskoopia | Spektroskoopia |
| Perekond | Process / pipeline | Process / pipeline |
| Tekkeaasta≠ | 1988 | 1954 |
| Looja≠ | Michael Karas | Otto Kratky |
| Tüüp≠ | Ionization and mass analysis technique | Synchrotron/X-ray technique |
| Algallikas≠ | Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301. DOI ↗ | Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press. link ↗ |
| Rööpnimetused≠ | MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry | SAXS, small-angle scattering |
| Seotud | 3 | 3 |
| Kokkuvõte≠ | 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. | Small-Angle X-ray Scattering (SAXS) is a solution-phase X-ray scattering technique that measures the overall shape and size of macromolecules and nanoparticles by analyzing scattering intensity at low angles (0.1-10 degrees). Developed by Kratky and colleagues in the 1950s, SAXS provides information about molecular radius, aggregation state, and overall shape without requiring crystallization or fixing, making it ideal for studying native protein conformations and dynamics. |
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