MAZURENKO, Stanislav. Predicting protein stability and solubility changes upon mutations: data perspective. ChemCatChem. Weinheim: Wiley-VCH GmbH, 2020, vol. 12, No 22, p. 5590-5598. ISSN 1867-3880. Available from: https://dx.doi.org/10.1002/cctc.202000933.
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Basic information
Original name Predicting protein stability and solubility changes upon mutations: data perspective
Authors MAZURENKO, Stanislav (643 Russian Federation, guarantor, belonging to the institution).
Edition ChemCatChem, Weinheim, Wiley-VCH GmbH, 2020, 1867-3880.
Other information
Original language English
Type of outcome Article in a journal
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW URL
RIV identification code RIV/00216224:14310/20:00117450
Organization Přírodovědecká fakulta – Repository – Repository
Doi http://dx.doi.org/10.1002/cctc.202000933
UT WoS 000565378700001
Keywords in English Database; Machine learning; Protein design; Protein engineering; Protein modifications
Links EF17_043/0009632, research and development project. EF17_050/0008496, research and development project. LM2015047, research and development project. LM2018121, research and development project. 857560, interní kód Repo.
Changed by Changed by: RNDr. Daniel Jakubík, učo 139797. Changed: 25/1/2022 14:11.
Abstract
Understanding mutational effects on protein stability and solubility is of particular importance for creating industrially relevant biocatalysts, resolving mechanisms of many human diseases, and producing efficient biopharmaceuticals, to name a few. Forin silicopredictions, the complexity of the underlying processes and increasing computational capabilities favor the use of machine learning. However, this approach requires sufficient training data of reasonable quality for making precise predictions. This minireview aims to summarize and scrutinize available mutational datasets commonly used for training predictors. We analyze their structure and discuss the possible directions of improvement in terms of data size, quality, and availability. We also present perspectives on the development of mutational data for accelerating the design of efficient predictors, introducing two new manually curated databases FireProt(DB)and SoluProtMut(DB)for protein stability and solubility, respectively.
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