Partially folded structure of monomeric bovine β-lactoglobulin

AbstractBovine 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