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Infrared Methods For Study Of Hemoglobin Reactions And Structures.
A. Dong, W. Caughey
Published 1994 · Chemistry, Medicine
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Publisher Summary This chapter presents the experimental approaches and interpretations of data for ligand spectra, microspectroscopy, thiol spectra, and amide I spectra. Methods using infrared (IR) spectroscopy provide important, often unique, means for the study of the reactions and structures of hemoglobins (Hb). The amide I bands, primarily because of the carbonyl groups in the peptide bonds that constitute the linkages between the amino acid residues of the Hb molecule, can be utilized for the qualitative and quantitative determination of α-helix, random, β-sheet, and turn secondary structures. Thus, the accurate measurement of an IR band at a given wavelength depends on the absorption of the medium as well as on protein concentration, intrinsic band intensity, and the distance through the sample traversed by the IR radiation. Improvements in IR instrumentation and in data analysis have greatly enhanced the sensitivity of the IR method applied to aqueous solutions.
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