Partially folded structure of monomeric bovine β-lactoglobulin

Henriette Molinari, Laura Ragona, Luca Varani, Giovanna Musco, Roberto Consonni, Lucia Zetta, Hugo L. Monaco

Research output: Contribution to journalArticle

Abstract

Bovine β-LG (β-lactoglobulin) has been studied under a variety of solution conditions by one- and two-dimensional NMR spectroscopy. At highly acidic pH (pH = 2) and low ionic strength the protein is present in a monomeric form, exhibiting a highly structured β-sheet core and less ordered regions as evidenced by both CD data and the NOESY spectra. Marginal protection was observed for most of the amide protons as a result of high conformational mobility. This structural state of β-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.

Original languageEnglish
Pages (from-to)237-243
Number of pages7
JournalFEBS Letters
Volume381
Issue number3
DOIs
Publication statusPublished - Mar 4 1996

Keywords

  • β-Lactoglobulin
  • CD
  • Locally unfolded structure
  • NMR

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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  • Cite this

    Molinari, H., Ragona, L., Varani, L., Musco, G., Consonni, R., Zetta, L., & Monaco, H. L. (1996). Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Letters, 381(3), 237-243. https://doi.org/10.1016/0014-5793(96)00100-7