Abstract
Mutant proteins are useful for study on the mechanism of protein stability. However, it is difficult to evaluate the changes in stability due to mutation, because contributions of amino acid residues to the conformational stability differ depending on their locations even if the same residues are substituted. In order to evaluate each contribution of several factors responsible for protein stability, we determined the crystal structures and measured the protein stability for more than a hundred of mutant human lysozymes. Analyzing this structure/stability database, the parameters of each stabilization factor, such as hydrophobic effect and hydrogen bond, could be estimated. These parameters are available for understanding the thermostabilization mechanism of the proteins from hyperthermophiles and for the computer-aided drug design.
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