J 2021

FireProt(DB): database of manually curated protein stability data

ŠTOURAČ, Jan; Juraj DUBRAVA; Miloš MUSIL; Jana HORÁČKOVÁ; Jiří DAMBORSKÝ et. al.

Basic information

Original name

FireProt(DB): database of manually curated protein stability data

Authors

ŠTOURAČ, Jan (203 Czech Republic, belonging to the institution); Juraj DUBRAVA (203 Czech Republic); Miloš MUSIL (203 Czech Republic, belonging to the institution); Jana HORÁČKOVÁ (203 Czech Republic, belonging to the institution); Jiří DAMBORSKÝ (203 Czech Republic, guarantor, belonging to the institution); Stanislav MAZURENKO (643 Russian Federation, belonging to the institution) and David BEDNÁŘ (203 Czech Republic, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford University Press, 2021, 0305-1048

Other information

Language

English

Type of outcome

Article in a journal

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

is not subject to a state or trade secret

References:

RIV identification code

RIV/00216224:14310/21:00119185

Organization

Přírodovědecká fakulta – Repository – Repository

UT WoS

000608437800041

EID Scopus

2-s2.0-85099428147

Keywords in English

SEQUENCE; PREDICTION; VARIANTS

Links

EF17_043/0009632, research and development project. EF19_074/0012727, research and development project. GJ20-15915Y, research and development project. LM2018121, research and development project. TN01000013, research and development project. 857560, interní kód Repo.
Changed: 16/2/2023 04:23, RNDr. Daniel Jakubík

Abstract

V originále

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.

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