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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....

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Detalles Bibliográficos
Autores principales: Buß, Oliver, Rudat, Jens, Ochsenreither, Katrin
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2018
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.
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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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