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Dikroisme Sirkular×MALDI-TOF×
BidangSpektroskopiSpektroskopi
KeluargaProcess / pipelineProcess / pipeline
Tahun asal19691988
PencetusJean-Claude FasmanMichael Karas
TipeSpectroscopic methodIonization and mass analysis technique
Sumber perintisGreenfield, 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 ↗
AliasCD spectroscopy, circular dichroism, CD analysisMALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry
Terkait33
RingkasanCircular 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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ScholarGateBandingkan metode: Circular Dichroism · MALDI-TOF. Diakses 2026-06-18 dari https://scholargate.app/id/compare