A critical evaluation of the predicted and X-ray structures of α-Lactalbumin

K. Ravi Acharya, David I. Stuart, David C. Phillips, Harold A. Scheraga

Research output: Contribution to journalArticlepeer-review


The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browne et al. (1969) and later by Warme et al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blake et al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharya et al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1-95, 1.1 Å).

Original languageEnglish
Pages (from-to)549-563
Number of pages15
JournalJournal of Protein Chemistry
Issue number5
Publication statusPublished - 1 Oct 1990


  • α-Lactalbumin
  • computer modeling
  • lysozyme
  • X-ray crystallography

ASJC Scopus subject areas

  • Biochemistry


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