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Secondary structural changes in the intact and the disulfide Bridges cleaved β-lactoglobulin A and B in solutions of urea, guanidine hydrochloride, and sodium dodecyl sulfate

Journal of Protein Chemistry volume 8, pages 487–494 (1989)Cite this article

Abstract

The relative proportions of α-helix, β-sheet, and unordered form in β-lactoglobulin A and B were examined in solutions of urea, guanidine, and sodium dodecyl sulfate (SDS). In the curve-fitting method of circular dichroism (CD) spectra, the reference spectra of the corresponding structures determined by Chen et al. (1974) were modified essentially according to the secondary structure of β-lactoglobulin B predicted by Creamer et al. (1983), i.e., that the protein has 17% α-helix and 41% β-sheet. The two variants showed no appreciable difference in structural changes. The reduction of disulfide bridges in the proteins increased β-sheet up to 48% but did not affect the α-helical proportion. The α-helical proportions of nonreduced β-lactoglobulin A and B were not affected below 2 M guanidine or below 3 M urea, but those of the reduced proteins began to decrease in much lower concentrations of these denaturants. By contrast, the α-helical proportions of the nonreduced and reduced proteins increased to 40–44% in SDS. The β-sheet proportions of both nonreduced and reduced proteins, which remained unaffected even in 6 M guanidine and 9 M urea, decreased to 24–25% in SDS.

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  1. Department of Applied Chemistry, Okayama University of Science, 700, Okayama, Japan

    Kunio Takeda & Yoshiko Moriyama

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  1. Kunio Takeda
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  2. Yoshiko Moriyama
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Takeda, K., Moriyama, Y. Secondary structural changes in the intact and the disulfide Bridges cleaved β-lactoglobulin A and B in solutions of urea, guanidine hydrochloride, and sodium dodecyl sulfate. J Protein Chem 8, 487–494 (1989). https://doi.org/10.1007/BF01026433

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  • DOI: https://doi.org/10.1007/BF01026433

Key words

  • β-lactoglobulin A
  • β-lactoglobulin B
  • secondary structure
  • CD
  • SDS