เปรียบเทียบวิธี

	MALDI-TOF	Circular Dichroism	FT-ICR Mass Spectrometry
สาขาวิชา	สเปกโทรสโกปี	สเปกโทรสโกปี	สเปกโทรสโกปี
ตระกูล	Process / pipeline	Process / pipeline	Process / pipeline
ปีกำเนิด	1988	1969	1974
ผู้ริเริ่ม	Michael Karas	Jean-Claude Fasman	Alan Marshall
ประเภท	Ionization and mass analysis technique	Spectroscopic method	Mass spectrometry technique
แหล่งต้นตำรับ	Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.	Comisarow, M. B., & Marshall, A. G. (1974). Fourier transform ion cyclotron resonance spectroscopy. Chemical Physics Letters, 25(2), 282-283.
ชื่อเรียกอื่น	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
ที่เกี่ยวข้อง	3	3	4
สรุป	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.