QUANTITATION OF THE ACCESSIBLE SURFACE OF GLOBULAR-PROTEINS BY TRITIUM PLANIGRAPHY

Tritium planigraphy was used to quantitate ''accessible surface'' for globular proteins. An experimental dependence was obtained for the pro bability of atomic tritium interaction with a series of globular prote ins whose accessible surface areas had been calculated from the data o f X-ray structural analysis. Using the data on the reactivity of indiv idual amino acid residues, a method is proposed for determining the ac cessible surface area of some types of amino acid residues in globular proteins. This approach was used to quantitate the accessible surface of pike parvalbumin III.