Přehled o publikaci
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.