Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin.

@article{Qin1999FunctionalIO,
  title={Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin.},
  author={Baomin Qin and Maria C. Bewley and Lawrence K. Creamer and Edward N Baker and Geoffrey B Jameson},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 1},
  pages={75-83}
}
The structure of the trigonal crystal form of bovine beta-lactoglobulin variant B at pH 7.1 has been determined by X-ray diffraction methods at a resolution of 2.22 A and refined to values for R and Rfree of 0.239 and 0.286, respectively. By comparison with the structure of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 7.1, which was determined previously [Qin BY et al., 1998, Biochemistry 37:14014-14023], the structural consequences of the sequence differences D64G and… CONTINUE READING

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