Pages: 1-9

Abstract

There are many methods to choose mutations that increase the constancy of proteins, including rational design, functional screening of accidentally generated mutant libraries, and comparison of naturally occurring similar proteins. The protein engineer’s toolbox is expanding and the number of successful instances of engineered protein constancy is increasing. Still, the selection of heat constancy mutations is not a standard process. Selection is complicated by lack of knowledge of the process that turns into thermal inactivation and by the fact that proteins employ a large variety of structural tricks to get constancy.