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Study on the Effect of Ultrasound on the Secondary Structure of BSA by FTIR

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Structure changes of bovine serum albumin (BSA) under ultrasound treatment were studied using Fourier transform infrared spectroscopy (FTIR) and fluorescence spectroscopy. The largest emission peak of BSA solution’s fluorescence spectra shifted in blue orientation, indicating that the environment of the Trp residues in BSA had altered with ultrasound treatment. The fluorescence intensity of the solution has also decreased with ultrasound, which showed fluorescence quenching effect and the conformation changes of the BSA. The relative contents of α-helix, β-fold, β-turn and random coil under different ultrasound treatment power and time were quantitatively determined via analysis of the amide changes of infrared spectra of BSA using curve fitting method, the secondary structure of BSA had variation trend from α-helix to β-sheet, however, the relative contents random coil had not significant change.
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Keywords: Bovine serum album; FTIR; Secondary structure; Ultrasound

Document Type: Research Article

Publication date: 01 August 2010

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  • Spectroscopy and Spectral Analysis, founded in 1981, is sponsored by the Chinese Central Iron & Steel Research Institute. "Spectroscopy and Spectral Analysis" has been indexed in SCI(1999), Ei(1992), MEDLINE(1999), and AJ (1999). "Spectroscopy and Spectral Analysis" publishes original contributions on various fields in Spectroscopy, including research results on laser spectroscopy, IR, Ramn, UV/Vis, Optical Emission, Absorption and Fluorescence spectroscopy, X-ray Fluorescence, and Spectrochemical Analysis, as well as Reseach paper, Research notes, Experimental Technique and Instrument, Review and Progress on the latest development of spectroscopy and spectrochemical anlysis, etc. "Spectroscopy and Spectral Analysis" is published monthly by Peking University Press with book sizes of large 16-mo format , and 292 pages per issue.
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