Author： Kirsch Joseph L. Koenig Jack L.
Publisher： Society for Applied Spectroscopy
ISSN： 0003-7028
Source： Applied Spectroscopy, Vol.43, Iss.3, 1989-03, pp. : 445-451
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Abstract
The FT-IR spectra of γ-globulin, chymotrypsin, serum albumin, and β-lactoglobulin were collected in aqueous buffer solutions at different temperatures. A least-squares subtraction algorithm was used to subtract the interfering water bands in the amide I, II, and III frequency regions. The spectra of the protein amide I and II bands were deconvoluted with the use of Fourier self-deconvolution and a Lorentzian curve fit process, and band assignments were made for the α helix, β pleated sheet, and disordered or turns structures of the proteins. Factor analysis was applied to the variable-temperature protein spectra, and the compositions with respect to the different types of secondary structures were calculated.
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