Masking of some charged groups in a protein with beta-structure

Reactivity of amino groups, phenoxy groups of tyrosine residues and some other charged groups of Tricoplusia ni granulosis virus granulin, which had rigid subunit structure abundant in beta-configuration, was investigated. It was found that there were nonreactive alpha-amino, phenoxy and some other groups in the native protein, and that they became reactive after an alkaline treatment which brought about conformational change of the protein to a random structure. The possibility of the contribution of the beta-structure for the masking of these residues is discussed.