Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer.

@article{Uhrnov2000StructuralCA,
  title={Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer.},
  author={Stanislava Uhr{\'i}nov{\'a} and Mark H Smith and Geoffrey B Jameson and Du{\vs}an Uhr{\'i}n and Lindsay Sawyer and Paul N. Barlow},
  journal={Biochemistry},
  year={2000},
  volume={39 13},
  pages={3565-74}
}
We have used NMR spectroscopy to determine the three-dimensional (3D) structure, and to characterize the backbone dynamics, of a recombinant version of bovine beta-lactoglobulin (variant A) at pH 2. 6, where the protein is a monomer. The structure of this low-pH form of beta-lactoglobulin is very similar to that of a subunit within the dimer at pH 6.2. The root-mean-square deviation from the pH 6.2 (crystal) structure, calculated for backbone atoms of residues 6-160, is approximately 1.3 A… CONTINUE READING

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