FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
- PMID: 30275935
- PMCID: PMC6158775
- DOI: 10.1016/j.csbj.2018.01.002
FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
Abstract
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.
Keywords: Enzyme engineering; Fold-X; FoldX; Protein engineering; Protein stabilization; Thermostability.
References
-
- Newman J.D., Turner A.P.F. Home blood glucose biosensors: a commercial perspective. Biosens Bioelectron. 2005;20:2435–2453. - PubMed
-
- Capdevila J., Elez E., Macarulla T., Ramos F.J., Ruiz-Echarri M., Tabernero J. Anti-epidermal growth factor receptor monoclonal antibodies in cancer treatment. Cancer Treat Rev. 2009;35:354–363. - PubMed
-
- Savile C.K., Janey J.M., Mundorff E.C., Moore J.C., Tam S., Jarvis W.R. Biocatalytic asymmetric synthesis of chiral amines from ketones applied to sitagliptin manufacture. Science. 2010;329:305–309. - PubMed
-
- Pollard D.J., Woodley J.M. Biocatalysis for pharmaceutical intermediates: the future is now. Trends Biotechnol. 2007;25:66–73. - PubMed
Publication types
LinkOut - more resources
Full Text Sources
Other Literature Sources