Partially folded structure of monomeric bovine β‐lactoglobulin
- 2 March 1996
- journal article
- Published by Wiley in FEBS Letters
- Vol. 381 (3), 237-243
- https://doi.org/10.1016/0014-5793(96)00100-7
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.Keywords
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