השוואת שיטות

	דיכרואיזם מעגלי	MALDI-TOF
תחום	ספקטרוסקופיה	ספקטרוסקופיה
משפחה	Process / pipeline	Process / pipeline
שנת המקור	1969	1988
הוגה השיטה	Jean-Claude Fasman	Michael Karas
סוג	Spectroscopic method	Ionization and mass analysis technique
מקור מכונן	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.	Karas, M., & Hillenkamp, F. (1988). Laser desorption ionization of proteins with molecular masses exceeding 10,000 daltons. Analytical Chemistry, 60(20), 2299-2301.
כינויים	CD spectroscopy, circular dichroism, CD analysis	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry
קשורות	3	3
תקציר	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.	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.