2004年
Heat-Induced Secondary Structure and Conformation Change of Bovine Serum Albumin investigated by Fourier-Transform Infrared Spectroscopy
Biochemistry
- ,
- 巻
- 43, 11526-11532
- 号
- 開始ページ
- 11526
- 終了ページ
- 11532
- DOI
- 10.1021/bi0489154
Fourier transform infrared (FT-IR) spectra were measured for an aqueous solution (pD = 5.40) of defatted monomer bovine serum albumin (BSA) over a temperature range of 25-90 °C to investigate temperature-induced secondary structure and conformation changes. The curve fitting method combined with the Fourier self-deconvolution technique allowed us to explore details of the secondary structure and conformation changes in defatted BSA. Particularly striking in the FT-IR spectra was an observation of the formation of an irreversible intermolecular β-sheet of BSA on heating above 70 °C. A band at 1630 cm-1 in the spectra was assigned to short-segment chains connecting α-helical segments. The transition temperature for the short-segment chains connecting α-helical segments is lower by 17-18 °C, when compared to those of the α-helix, turn, and intermolecular β-sheet structures of BSA, suggesting that the α-helix and turn structures of BSA are cooperatively denatured on heating. Moreover, the results give an important feature in heat-induced denaturation of BSA that the conformation changes occur twice around both 57 and 75 °C. The appearance of two peaks is interpreted by the co
- リンク情報
- ID情報
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- DOI : 10.1021/bi0489154
- ISSN : 0006-2960
- CiNii Articles ID : 20000934465
- PubMed ID : 15350138