Comparative Adsorption Studies with Synthetic, Structural Stability and Charge Mutants of Bacteriophage T4 Lysozyme.
We have purified wild type, three structural stability mutants and four charge mutants of bacteriophage T4 lysozyme from E. coli strains harboring desired expression vectors. Structural stability mutants were produced by substitution of the isoleucine at amino acid position three, yielding a set of proteins with stabilities ranging from 1.2 kcal/mol greater, to 2.8 kcal/mol less, than that of the