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FoldX as Protein Engineering Tool: Better Than Random Based Approaches?
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....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Research Network of Computational and Structural Biotechnology
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158775/ https://www.ncbi.nlm.nih.gov/pubmed/30275935 http://dx.doi.org/10.1016/j.csbj.2018.01.002 |
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author | Buß, Oliver Rudat, Jens Ochsenreither, Katrin |
author_facet | Buß, Oliver Rudat, Jens Ochsenreither, Katrin |
author_sort | Buß, Oliver |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6158775 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Research Network of Computational and Structural Biotechnology |
record_format | MEDLINE/PubMed |
spelling | pubmed-61587752018-10-01 FoldX as Protein Engineering Tool: Better Than Random Based Approaches? Buß, Oliver Rudat, Jens Ochsenreither, Katrin Comput Struct Biotechnol J Short Survey 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. Research Network of Computational and Structural Biotechnology 2018-02-03 /pmc/articles/PMC6158775/ /pubmed/30275935 http://dx.doi.org/10.1016/j.csbj.2018.01.002 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Short Survey Buß, Oliver Rudat, Jens Ochsenreither, Katrin FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title | FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title_full | FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title_fullStr | FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title_full_unstemmed | FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title_short | FoldX as Protein Engineering Tool: Better Than Random Based Approaches? |
title_sort | foldx as protein engineering tool: better than random based approaches? |
topic | Short Survey |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6158775/ https://www.ncbi.nlm.nih.gov/pubmed/30275935 http://dx.doi.org/10.1016/j.csbj.2018.01.002 |
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