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The structural changes occurring during the interaction between β-lactoglobulin (BLG), the major whey protein, and bovine submaxillary mucin (BSM), a major salivary protein, were studied using high and low field Nuclear Magnetic Resonance (NMR), Dynamic Light Scattering (DLS), and Circular Dichroism (CD) spectroscopy. The zeta potentials of the proteins were also measured to provide information on...
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...
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