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Selection of mutations for increased protein stability

2002; Elsevier BV; Volume: 13; Issue: 4 Linguagem: Inglês

10.1016/s0958-1669(02)00325-7

1879-0429

Bertus van den Burg, Vincent G. H. Eijsink,

Protein purification and stability

There are many ways to select mutations that increase the stability of proteins, including rational design, functional screening of randomly generated mutant libraries, and comparison of naturally occurring homologous proteins. The protein engineer's toolbox is expanding and the number of successful examples of engineered protein stability is increasing. Still, the selection of thermostable mutations is not a standard process. Selection is complicated by lack of knowledge of the process that leads to thermal inactivation and by the fact that proteins employ a large variety of structural tricks to achieve stability.