A critical evaluation of the predicted and X-ray structures of alpha-lactalbumin.

Journal article

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 alpha-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-di...

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Authors: Acharya, K; Stuart, D; Phillips, D; Scheraga, H

• Publication status: Published
• Publisher: Kluwer Academic Publishers-Plenum Publishers
• Journal: Journal of protein chemistry
• Volume: 9
• Issue: 5
• Pages: 549-563
• Publication date: 1990-10-01
• DOI: 10.1007/bf01025008
• EISSN: 1573-4943
• ISSN: 0277-8033
• Language: English
• Keywords: Lactalbumin; Species Specificity; Protein Conformation; Binding Sites; X-Ray Diffraction; Cattle; Papio; Computer Simulation; Humans; Calcium; Amino Acid Sequence; Molecular Sequence Data; Models, Molecular; Animals; Proline