Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Stourac, Jan, Dubrava, Juraj, Musil, Milos, Horackova, Jana, Damborsky, Jiri, Mazurenko, Stanislav, Bednar, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2020
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
_version_ 1783631217156947968
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
work_keys_str_mv AT stouracjan fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT dubravajuraj fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT musilmilos fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT horackovajana fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT damborskyjiri fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT mazurenkostanislav fireprotdbdatabaseofmanuallycuratedproteinstabilitydata
AT bednardavid fireprotdbdatabaseofmanuallycuratedproteinstabilitydata