Protein function evolution stability improvement

There have been many attempts to improve protein stability and protein properties, utilizing methods such as random mutagenesis, directed evolution, and rational protein design approaches. In general, these methods are far from straightforward and can be time-consuming. In addition, the stabilization of proteins without loss of function is not a trivial problem. 

Basic research will further develop techniques for studies on electron transfer phenomena in biological macromolecules. In applied research, the optimization of the direct electron transfer between bioelements and electrodes is dominant. Improvement of DET is anticipated by a better orientation and binding of redox proteins and redox enzymes and the stabilization of the bioelement. Simultaneously an increased stability is pursued. The employed genetic methods for protein engineering are based oti rational design and directed evolution. With the advance of analytical methods and a better knowledge of the structure/functional relationship of DET in redox proteins and redox enzymes the engineering of electron transfer pathways within proteins will become feasible. 

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