Abstract
Mutant proteins are useful for study of protein stability. However, it is difficult to explain the changes in stability due to mountain, because contributions of amino acid residues to the conformational stability are quite different, depending on their location. In order to quantify directly the contribution of several factors to the conformational stability of a protein, we determined the thermodynamic parameters of denaturation and the crystal structures for more than 60 mutant human lysozymes. Analyzing this database (stability/structure database), the contribution of some factors to conformational stability of a protein, such as hydrophobic effect, hydrogen bond, and water molecule, could be estimated.
