Monomeric bovine β‐lactoglobulin adopts a β‐barrel fold at pH 2

FEBS Letters

Zetta, L²  Ragona, L²  Fogolari, F³  De Kruif, K.G¹  Molinari, H³  Romagnoli, S³ 

[1] Department of Biophysical Chemistry and Technology, Netherlands Institute for Dairy Research (NIZO), 6710 BA Ede, The Netherlands;Laboratorio NMR, CNR, ICM, Via Ampere 56, 20131 Milan, Italy;Istituto Policattedra, Università degli Studi di Verona, Strada Le Grazie, 37100 Verona, Italy

关键词: Bovine β-lactoglobulin;    Nuclear magnetic resonance;    Structure calculation;    Surface electrostatic property;   

DOI  :  10.1016/S0014-5793(98)00936-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown