SoluProtMutDB: A manually curated database of protein solubility changes upon mutations
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F22%3A00078809" target="_blank" >RIV/00159816:_____/22:00078809 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/00216305:26230/22:PU146770 RIV/00216224:14310/22:00130114
Výsledek na webu
<a href="https://www.sciencedirect.com/science/article/pii/S2001037022005025?via%3Dihub" target="_blank" >https://www.sciencedirect.com/science/article/pii/S2001037022005025?via%3Dihub</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.csbj.2022.11.009" target="_blank" >10.1016/j.csbj.2022.11.009</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
SoluProtMutDB: A manually curated database of protein solubility changes upon mutations
Popis výsledku v původním jazyce
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 33000 measurements of 17000 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. (C) 2022 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Název v anglickém jazyce
SoluProtMutDB: A manually curated database of protein solubility changes upon mutations
Popis výsledku anglicky
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 33000 measurements of 17000 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. (C) 2022 The Author(s). Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2022
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Computational and Structural Biotechnology Journal
ISSN
2001-0370
e-ISSN
—
Svazek periodika
20
Číslo periodika v rámci svazku
2022
Stát vydavatele periodika
SE - Švédské království
Počet stran výsledku
9
Strana od-do
6339-6347
Kód UT WoS článku
001043880900004
EID výsledku v databázi Scopus
—