2020
DOI: 10.1002/cctc.202000933
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Predicting protein stability and solubility changes upon mutations: data perspective

Abstract: This publication is part of a Special Collection on "Data Science in Catalysis" Please check the ChemCatChem homepage for more articles in the collection.

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Cited by 26 publications
(23 citation statements)
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References 89 publications
(140 reference statements)
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“…The development of novel algorithms and soware tools for rational engineering of protein loops is highly desirable, but still challenging. New experimental data 51 and better understanding of structure-stability relationships are also essential premises for developing more reliable predictive models by machine learning. 52…”
Section: Discussionmentioning
confidence: 99%
“…The development of novel algorithms and soware tools for rational engineering of protein loops is highly desirable, but still challenging. New experimental data 51 and better understanding of structure-stability relationships are also essential premises for developing more reliable predictive models by machine learning. 52…”
Section: Discussionmentioning
confidence: 99%
“…Several types of search queries may be of interest to the users. The first one relates to data filtering by values ( 10 ). Typically, software developers filter out the data collected at extreme pH (<6 or >8) due to changes in charged states for ionizable residues.…”
Section: Resultsmentioning
confidence: 99%
“…Overall we confirmed the presence of the well-known mutation-type imbalances in all three datasets including the symmetric and curated datasets. Apparently, compilation of a balanced dataset requires attention to a list of features, 48 otherwise ensuring a symmetric distribution and/or removing of large redundancies does not necessarily solve all of the quality issues.…”
Section: Resultsmentioning
confidence: 99%