Circular-dichroism spectra of a barley 1,3-beta-glucanase were analysed by two methods. The combined results predict 36-40% helix and 15-18% beta-structure in the protein. Prediction of secondary-structural features on the basis of amino acid sequence information yielded overall helix and beta-structure contents of 37% and 19% respectively. Comparison of the predicted structural elements along the barley 1,3-beta-glucanase with those of three related plant glucanases and a yeast glucanase suggest a close similarity in secondary structure among the five proteins. Consideration is given to the potential importance of certain amino acids which are conserved in these five glucanases.
