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Partially folded structure of monomeric bovine beta-lactoglobulin
H Molinari1, L Ragona, L Varani
1Istituto Policattedra della Facoltà di Scienze, Universitá degli Studidi Verona, Italy.
Abstract:
Bovine beta-LG (beta-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 beta-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 beta-LG may be considered as an attractive model for a partially folded structure occurring late in the folding process of the protein.