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SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations

Protein solubility is an attractive engineering target primarily due to its relation to yields in protein production and manufacturing. Moreover, better knowledge of the mutational effects on protein solubility could connect several serious human diseases with protein aggregation. However, we have l...

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Autores principales: Velecký, Jan, Hamsikova, Marie, Stourac, Jan, Musil, Milos, Damborsky, Jiri, Bednar, David, Mazurenko, Stanislav
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9678803/
https://www.ncbi.nlm.nih.gov/pubmed/36420168
http://dx.doi.org/10.1016/j.csbj.2022.11.009
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author Velecký, Jan
Hamsikova, Marie
Stourac, Jan
Musil, Milos
Damborsky, Jiri
Bednar, David
Mazurenko, Stanislav
author_facet Velecký, Jan
Hamsikova, Marie
Stourac, Jan
Musil, Milos
Damborsky, Jiri
Bednar, David
Mazurenko, Stanislav
author_sort Velecký, Jan
collection PubMed
description Protein solubility is an attractive engineering target primarily due to its relation to yields in protein production and manufacturing. Moreover, better knowledge of the mutational effects on protein solubility could connect several serious human diseases with protein aggregation. However, we have limited understanding of the protein structural determinants of solubility, and the available data have mostly been scattered in the literature. Here, we present SoluProtMut(DB) – the first database containing data on protein solubility changes upon mutations. Our database accommodates 33 000 measurements of 17 000 protein variants in 103 different proteins. The database can serve as an essential source of information for the researchers designing improved protein variants or those developing machine learning tools to predict the effects of mutations on solubility. The database comprises all the previously published solubility datasets and thousands of new data points from recent publications, including deep mutational scanning experiments. Moreover, it features many available experimental conditions known to affect protein solubility. The datasets have been manually curated with substantial corrections, improving suitability for machine learning applications. The database is available at loschmidt.chemi.muni.cz/soluprotmutdb.
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spelling pubmed-96788032022-11-22 SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations Velecký, Jan Hamsikova, Marie Stourac, Jan Musil, Milos Damborsky, Jiri Bednar, David Mazurenko, Stanislav Comput Struct Biotechnol J Data Article Protein solubility is an attractive engineering target primarily due to its relation to yields in protein production and manufacturing. Moreover, better knowledge of the mutational effects on protein solubility could connect several serious human diseases with protein aggregation. However, we have limited understanding of the protein structural determinants of solubility, and the available data have mostly been scattered in the literature. Here, we present SoluProtMut(DB) – the first database containing data on protein solubility changes upon mutations. Our database accommodates 33 000 measurements of 17 000 protein variants in 103 different proteins. The database can serve as an essential source of information for the researchers designing improved protein variants or those developing machine learning tools to predict the effects of mutations on solubility. The database comprises all the previously published solubility datasets and thousands of new data points from recent publications, including deep mutational scanning experiments. Moreover, it features many available experimental conditions known to affect protein solubility. The datasets have been manually curated with substantial corrections, improving suitability for machine learning applications. The database is available at loschmidt.chemi.muni.cz/soluprotmutdb. Research Network of Computational and Structural Biotechnology 2022-11-09 /pmc/articles/PMC9678803/ /pubmed/36420168 http://dx.doi.org/10.1016/j.csbj.2022.11.009 Text en © 2022 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Data Article
Velecký, Jan
Hamsikova, Marie
Stourac, Jan
Musil, Milos
Damborsky, Jiri
Bednar, David
Mazurenko, Stanislav
SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title_full SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title_fullStr SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title_full_unstemmed SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title_short SoluProtMut(DB): A manually curated database of protein solubility changes upon mutations
title_sort soluprotmut(db): a manually curated database of protein solubility changes upon mutations
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9678803/
https://www.ncbi.nlm.nih.gov/pubmed/36420168
http://dx.doi.org/10.1016/j.csbj.2022.11.009
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