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MALDI-TOF×圆二色性×
领域光谱学光谱学
方法族Process / pipelineProcess / pipeline
起源年份19881969
提出者Michael KarasJean-Claude Fasman
类型Ionization and mass analysis techniqueSpectroscopic method
开创性文献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 ↗
别名MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometryCD spectroscopy, circular dichroism, CD analysis
相关33
摘要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.
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ScholarGate方法对比: MALDI-TOF · Circular Dichroism. 于 2026-06-18 检索自 https://scholargate.app/zh/compare