FoldX as protein engineering tool: Better than random based approaches?

Publication date: Available online 3 February 2018 Source:Computational and Structural Biotechnology Journal Author(s): Oliver Buß, Jens Rudat, Katrin Ochsenreither Improving protein stability is an important goal for basic research as well as for clinical and industrial applications but no commonly accepted and widely used strategy for efficient engineering is known. Beside random approaches like error prone PCR or physical techniques to stabilize proteins, e.g. by immobilization, in silico approaches are gaining more attention to apply target-oriented mutagenesis. In this review different algorithms for the prediction of beneficial mutation sites to enhance protein stability are summarized and the advantages and disadvantages of FoldX are highlighted. The question whether the prediction of mutation sites by the algorithm FoldX is more accurate than random based approaches is addressed. Graphical abstract

Source: Computational and Structural Biotechnology Journal - February 7, 2018 Category: Biotechnology Source Type: research