| Literature DB >> 12323355 |
Bertus van den Burg1, Vincent G H Eijsink.
Abstract
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.Mesh:
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Year: 2002 PMID: 12323355 DOI: 10.1016/s0958-1669(02)00325-7
Source DB: PubMed Journal: Curr Opin Biotechnol ISSN: 0958-1669 Impact factor: 9.740