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  This repository contains data on the change in protein stability with a single mutation.
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  ## Attribution of Data Sources
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  - **Primary Source**: Tsuboyama, K., Dauparas, J., Chen, J. et al. Mega-scale experimental analysis of protein folding stability in biology and design. Nature 620, 434–444 (2023). [Link to the paper](https://www.nature.com/articles/s41586-023-06328-6)
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  ### Data Cleanup and Validation:
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  1. Filtering: The dataset has been curated to only include examples of single mutations.
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- 2. Consistency Check: Only rows with consistent mutation indication, aligned with both the base and mutated sequences, have been retained.
 
 
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  This repository contains data on the change in protein stability with a single mutation.
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+ There are two datasets:
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+ - [Sample dataset, ~100 datapoints](https://huggingface.co/datasets/Trelis/protein_stability_single_mutation_SAMPLE).
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+ - [Gated dataset, ~250k datapoints](https://huggingface.co/datasets/Trelis/protein_stability_single_mutation).
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  ## Attribution of Data Sources
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  - **Primary Source**: Tsuboyama, K., Dauparas, J., Chen, J. et al. Mega-scale experimental analysis of protein folding stability in biology and design. Nature 620, 434–444 (2023). [Link to the paper](https://www.nature.com/articles/s41586-023-06328-6)
 
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  ### Data Cleanup and Validation:
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  1. Filtering: The dataset has been curated to only include examples of single mutations.
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+ 2. Sequence mutations were extracted from the row names. Base mutations are labelled as 'base'.
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+ 3. Consistency Check: Only rows with a consistent 'mutation', aligned with both the base and mutated sequences from the raw data, have been retained.