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A dataset of protein variants with annotated with their experimental DDG values, collected and manually cleaned from the latest version of the ThermoMutDB database, consisting of 669 variants not included in the most widely used training datasets. It includes the protein structures (both wild-type and mutated) for the variants. Please refer to the original publication: Corrado Pancotti, Silvia Benevenuta, Giovanni Birolo, Virginia Alberini, Valeria Repetto, Tiziana Sanavia, Emidio Capriotti, Piero Fariselli, Predicting protein stability changes upon single-point mutation: a thorough comparison of the available tools on a new dataset, Briefings in Bioinformatics, Volume 23, Issue 2, March 2022, bbab555, https://doi.org/10.1093/bib/bbab555
{"references": ["Corrado Pancotti, Silvia Benevenuta, Giovanni Birolo, Virginia Alberini, Valeria Repetto, Tiziana Sanavia, Emidio Capriotti, Piero Fariselli, Predicting protein stability changes upon single-point mutation: a thorough comparison of the available tools on a new dataset,\u00a0Briefings in Bioinformatics, Volume 23, Issue 2, March 2022, bbab555,\u00a0https://doi.org/10.1093/bib/bbab555"]}
protein stability, single-point mutation, stability change, antisymmetry, machine learning
protein stability, single-point mutation, stability change, antisymmetry, machine learning
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