Comparar métodos

	Dicroísmo Circular	MALDI-TOF	SAXS
Área	Espectroscopia	Espectroscopia	Espectroscopia
Família	Process / pipeline	Process / pipeline	Process / pipeline
Ano de origem	1969	1988	1954
Autor original	Jean-Claude Fasman	Michael Karas	Otto Kratky
Tipo	Spectroscopic method	Ionization and mass analysis technique	Synchrotron/X-ray technique
Fonte seminal	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.	Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press.
Outros nomes	CD spectroscopy, circular dichroism, CD analysis	MALDI mass spectrometry, MALDI-TOF-MS, laser desorption mass spectrometry	SAXS, small-angle scattering
Relacionados	3	3	3
Resumo	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.	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.