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

Research output: Contribution to journalArticlepeer-review

460 Scopus citations


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
Issue number40
StatePublished - Oct 6 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry


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