ABSTRACT

Mutant proteins has been widely used in recent studies of biochemistry and molecular biology. However, single amino acid substitutions affect the protein stability and structure in various ways depending on the type and site of the mutations. We have constructed systematic and comprehensive mutant proteins of the human lysozyme and determined their thermodynamic parameters of denaturation and their crystal structures. The studies using such systematic mutant proteins allows us to determine how a substitution changes the stability and structure, what kind of factor contributes to the protein stability, and how much it contributes.