เปรียบเทียบวิธี

	แคลอริเมทรีแบบไทเทรตที่อุณหภูมิคงที่	Circular Dichroism
สาขาวิชา	สเปกโทรสโกปี	สเปกโทรสโกปี
ตระกูล	Process / pipeline	Process / pipeline
ปีกำเนิด	1989	1969
ผู้ริเริ่ม	Terrence Wiseman	Jean-Claude Fasman
ประเภท	Biophysical technique	Spectroscopic method
แหล่งต้นตำรับ	Wiseman, T., Williston, S., Brandts, J. F., & Lin, L. N. (1989). Rapid measurement of binding constants and heats of binding using a new titration calorimeter. Analytical Biochemistry, 179(1), 131-137.	Greenfield, N. J., & Fasman, G. D. (1969). Computed circular dichroism spectra for protein secondary structures. Biochemistry, 8(10), 4108-4116.
ชื่อเรียกอื่น	ITC, isothermal calorimetry, microcalorimetry	CD spectroscopy, circular dichroism, CD analysis
ที่เกี่ยวข้อง	3	3
สรุป	Isothermal Titration Calorimetry (ITC) is a thermodynamic technique that measures heat released or absorbed during biomolecular binding events at constant temperature. Developed by Wiseman and colleagues in 1989, ITC directly determines binding affinity (Kd), enthalpy (ΔH), and entropy (ΔS) in a single experiment, making it one of the most comprehensive methods for characterizing molecular interactions without requiring labels or immobilization.	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.