Monomeric bovine β‐lactoglobulin adopts a β‐barrel fold at pH 2
- 2 October 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 436 (2) , 149-154
- https://doi.org/10.1016/s0014-5793(98)00936-3
Abstract
We have determined a crude structure of the apo form of bovine β-lactoglobulin, a protein of 162 amino acid residues with a molecular mass of 18 kDa, at a low pH on the basis of data collected using only homonuclear 1H NMR spectroscopy. An ensemble of protein conformations was calculated with the distance-geometry algorithm for NMR applications (DYANA). The monomeric protein at low pH adopts a β-barrel fold, well-superimposable on the structure determined by X-ray crystallography for the dimer at physiological pH. NMR evidence suggests the presence of disordered loop regions and terminal segments. Structural differences between the monomer at pH 2 and the dimer at pH 7, obtained by X-ray crystallography, are discussed, paying particular attention to surface electrostatic properties, in view of the high charge state of the protein at low pH.Keywords
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