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FireProt(DB): database of manually curated protein stability data
The majority of naturally occurring proteins have evolved to function under mild conditions inside the living organisms. One of the critical obstacles for the use of proteins in biotechnological applications is their insufficient stability at elevated temperatures or in the presence of salts. Since...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778887/ https://www.ncbi.nlm.nih.gov/pubmed/33166383 http://dx.doi.org/10.1093/nar/gkaa981 |
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author | Stourac, Jan Dubrava, Juraj Musil, Milos Horackova, Jana Damborsky, Jiri Mazurenko, Stanislav Bednar, David |
author_facet | Stourac, Jan Dubrava, Juraj Musil, Milos Horackova, Jana Damborsky, Jiri Mazurenko, Stanislav Bednar, David |
author_sort | Stourac, Jan |
collection | PubMed |
description | The majority of naturally occurring proteins have evolved to function under mild conditions inside the living organisms. One of the critical obstacles for the use of proteins in biotechnological applications is their insufficient stability at elevated temperatures or in the presence of salts. Since experimental screening for stabilizing mutations is typically laborious and expensive, in silico predictors are often used for narrowing down the mutational landscape. The recent advances in machine learning and artificial intelligence further facilitate the development of such computational tools. However, the accuracy of these predictors strongly depends on the quality and amount of data used for training and testing, which have often been reported as the current bottleneck of the approach. To address this problem, we present a novel database of experimental thermostability data for single-point mutants FireProt(DB). The database combines the published datasets, data extracted manually from the recent literature, and the data collected in our laboratory. Its user interface is designed to facilitate both types of the expected use: (i) the interactive explorations of individual entries on the level of a protein or mutation and (ii) the construction of highly customized and machine learning-friendly datasets using advanced searching and filtering. The database is freely available at https://loschmidt.chemi.muni.cz/fireprotdb. |
format | Online Article Text |
id | pubmed-7778887 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-77788872021-01-06 FireProt(DB): database of manually curated protein stability data Stourac, Jan Dubrava, Juraj Musil, Milos Horackova, Jana Damborsky, Jiri Mazurenko, Stanislav Bednar, David Nucleic Acids Res Database Issue The majority of naturally occurring proteins have evolved to function under mild conditions inside the living organisms. One of the critical obstacles for the use of proteins in biotechnological applications is their insufficient stability at elevated temperatures or in the presence of salts. Since experimental screening for stabilizing mutations is typically laborious and expensive, in silico predictors are often used for narrowing down the mutational landscape. The recent advances in machine learning and artificial intelligence further facilitate the development of such computational tools. However, the accuracy of these predictors strongly depends on the quality and amount of data used for training and testing, which have often been reported as the current bottleneck of the approach. To address this problem, we present a novel database of experimental thermostability data for single-point mutants FireProt(DB). The database combines the published datasets, data extracted manually from the recent literature, and the data collected in our laboratory. Its user interface is designed to facilitate both types of the expected use: (i) the interactive explorations of individual entries on the level of a protein or mutation and (ii) the construction of highly customized and machine learning-friendly datasets using advanced searching and filtering. The database is freely available at https://loschmidt.chemi.muni.cz/fireprotdb. Oxford University Press 2020-11-09 /pmc/articles/PMC7778887/ /pubmed/33166383 http://dx.doi.org/10.1093/nar/gkaa981 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Database Issue Stourac, Jan Dubrava, Juraj Musil, Milos Horackova, Jana Damborsky, Jiri Mazurenko, Stanislav Bednar, David FireProt(DB): database of manually curated protein stability data |
title | FireProt(DB): database of manually curated protein stability data |
title_full | FireProt(DB): database of manually curated protein stability data |
title_fullStr | FireProt(DB): database of manually curated protein stability data |
title_full_unstemmed | FireProt(DB): database of manually curated protein stability data |
title_short | FireProt(DB): database of manually curated protein stability data |
title_sort | fireprot(db): database of manually curated protein stability data |
topic | Database Issue |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7778887/ https://www.ncbi.nlm.nih.gov/pubmed/33166383 http://dx.doi.org/10.1093/nar/gkaa981 |
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