Structural basis of the tanford transition of bovine β-lactoglobulin

Bin Y. Qin, Maria Bewley, Lawrence K. Creamer, Heather M. Baker, Edward N. Baker, Geoffrey B. Jameson

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Abstract

The structures of the trigonal crystal form of bovine β-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2.24, and 2.49 Å, respectively. The corresponding values for R (R(free)) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH- dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.

Original languageEnglish (US)
Pages (from-to)14014-14023
Number of pages10
JournalBiochemistry
Volume37
Issue number40
DOIs
StatePublished - Oct 6 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry

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    Qin, B. Y., Bewley, M., Creamer, L. K., Baker, H. M., Baker, E. N., & Jameson, G. B. (1998). Structural basis of the tanford transition of bovine β-lactoglobulin. Biochemistry, 37(40), 14014-14023. https://doi.org/10.1021/bi981016t