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

Comput Struct Biotechnol J

Institute of Process Engineering in Life Sciences, Section II: Technical Biology, Karlsruhe Institute of Technology, Karlsruhe, Germany.

Published: February 2018

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.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158775PMC
http://dx.doi.org/10.1016/j.csbj.2018.01.002DOI Listing

Publication Analysis

Top Keywords

random based
8
protein stability
8
mutation sites
8
foldx protein
4
protein engineering
4
engineering tool
4
tool better
4
better random
4
based approaches?
4
approaches? improving
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!