So sánh phương pháp

	XANES	ATR-FTIR	SAXS
Lĩnh vực	Quang phổ học	Quang phổ học	Quang phổ học
Họ	Process / pipeline	Process / pipeline	Process / pipeline
Năm ra đời	1975	1961	1954
Người khởi xướng	Peter Lee	Joop Fahrenfort	Otto Kratky
Loại	Synchrotron technique	Vibrational spectroscopy technique	Synchrotron/X-ray technique
Công trình gốc	Lee, P. A., & Pendry, J. B. (1975). Theory of extended x-ray absorption fine structure. Physical Review B, 11(8), 2795-2811.	Harrick, N. J. (1960). Study of physics of internal reflection from metals. Journal of Physics and Chemistry of Solids, 13(2), 143-155.	Glatter, O., & Kratky, O. (1982). Small Angle X-ray Scattering. Academic Press.
Tên gọi khác	XANES spectroscopy, near-edge X-ray absorption	ATR-IR, attenuated total reflectance, FTIR spectroscopy	SAXS, small-angle scattering
Liên quan	3	3	3
Tóm tắt	X-ray Absorption Near Edge Structure (XANES) is a synchrotron X-ray spectroscopy technique that measures the electronic and geometric structure around a specific atom by analyzing the X-ray absorption spectrum within about 50 eV of an absorption edge. Developed by Lee and Pendry in 1975, XANES is complementary to EXAFS and reveals valence state, local symmetry, and unoccupied orbital structure through near-threshold features and resonances.	Attenuated Total Reflectance (ATR) Fourier Transform Infrared (FTIR) spectroscopy is a variant of conventional FTIR that measures infrared absorption through evanescent-wave interrogation of samples in direct contact with a high-refractive-index crystal. Developed by Harrick and Fahrenfort in the 1960s, ATR-FTIR is now the dominant form of FTIR spectroscopy, enabling rapid, non-destructive characterization of organic compounds, polymers, coatings, and biological materials without extensive sample preparation.	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.