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Quantitative Estimation of α-Helix Coil Content in Bovine Serum Albumin by Fourier Transform-Infrared Spectroscopy

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Heat denaturation of albumin aqueous solution enables us to control the α-helix content to a reasonable level, and denatured albumin, whose conformation is different, can be obtained. Fourier transform-infrared absorption spectra in the amide I, II, and III band regions of these albumins have been measured and compared with each other. As a result, the characteristic frequencies associated with each conformation of α-helix, β-sheet, and random structure have been observed; moreover it has been newly proved that the intensity ratio of the amide II band to the amide I band depends on the α-helix content in albumin. In this paper, we demonstrate that this intensity ratio is very useful for quantitative estimation of α-helix content in albumin and apply this method to analysis of ATR spectra of albumin adsorbed on polyethylene surface.

Keywords: ATR spectroscopy; Analysis for secondary structure of protein; Infrared; Surface analysis; UV-visible spectroscopy

Document Type: Research Article

DOI: http://dx.doi.org/10.1366/0003702874448049

Affiliations: Department of Industrial Chemistry, Faculty of Engineering, University of Tokyo, Hongo Bunkyo-ku Tokyo 113, Japan

Publication date: July 1, 1987

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