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Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy.
- Source :
-
Biochemistry [Biochemistry] 2004 Sep 14; Vol. 43 (36), pp. 11526-32. - Publication Year :
- 2004
-
Abstract
- 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 degrees 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 beta-sheet of BSA on heating above 70 degrees C. A band at 1630 cm(-1) in the spectra was assigned to short-segment chains connecting alpha-helical segments. The transition temperature for the short-segment chains connecting alpha-helical segments is lower by 17-18 degrees C, when compared to those of the alpha-helix, turn, and intermolecular beta-sheet structures of BSA, suggesting that the alpha-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 degrees C. The appearance of two peaks is interpreted by the collapse of the N-terminal BSA domain due to the crevice in the vicinity between domains I and II at low-temperature transition and by the change in cooperative unit composed of the other two BSA domains at high-temperature transition.
- Subjects :
- Animals
Cattle
Phase Transition
Protein Conformation
Protein Denaturation
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Serum Albumin, Bovine metabolism
Temperature
Hot Temperature
Serum Albumin, Bovine chemistry
Spectroscopy, Fourier Transform Infrared methods
Spectroscopy, Fourier Transform Infrared statistics & numerical data
Subjects
Details
- Language :
- English
- ISSN :
- 0006-2960
- Volume :
- 43
- Issue :
- 36
- Database :
- MEDLINE
- Journal :
- Biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 15350138
- Full Text :
- https://doi.org/10.1021/bi0489154