The secondary structure of milk proteins and their biological function (original) (raw)

Journal of dairy science, 1993

Abstract

A brief overview is given of the methods of determining and predicting secondary structure in proteins. The secondary structures of the milk serum proteins, lactoferrin, alpha-lactalbumin, lysozyme, and beta-lactoglobulin, as determined by x-ray crystallography, are compared with the results of a joint prediction method. This comparison evaluates critically the degree of success achieved and helps define what can reasonably be expected from a prediction in the absence of a known structure. The value of supplementary information from spectroscopic methods and the use of templates and sequence information from related proteins in improving the confidence of predictions are illustrated. One point that emerges is the general overprediction of helix content by the joint prediction method such that, for an all-beta protein such as beta-lactoglobulin, the method of Garnier, Osguthorpe, and Robson, applied with the correctly selected decision constants, provides a somewhat better approach. ...

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