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FoldX as Protein Engineering Tool: Better Than Random Based Approaches?

Buß, Oliver 1; Rudat, Jens 1; Ochsenreither, Katrin ORCID iD icon 1
1 Institut für Bio- und Lebensmitteltechnik (BLT), Karlsruher Institut für Technologie (KIT)

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.


Verlagsausgabe §
DOI: 10.5445/IR/1000082044
Veröffentlicht am 16.04.2018
Originalveröffentlichung
DOI: 10.1016/j.csbj.2018.01.002
Scopus
Zitationen: 143
Web of Science
Zitationen: 127
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Zitationen: 180
Cover der Publikation
Zugehörige Institution(en) am KIT Institut für Bio- und Lebensmitteltechnik (BLT)
Publikationstyp Zeitschriftenaufsatz
Publikationsjahr 2018
Sprache Englisch
Identifikator ISSN: 2001-0370
urn:nbn:de:swb:90-820445
KITopen-ID: 1000082044
Erschienen in Computational and structural biotechnology journal
Verlag Elsevier
Band 16
Seiten 25–33
Bemerkung zur Veröffentlichung Gefördert durch den KIT-Publikationsfonds
Nachgewiesen in Scopus
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Web of Science
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