ThermoMutDB

ThermoMutDB provides a curated database of experimental thermodynamic parameters for wild-type and mutant proteins to support analysis and prediction of mutation-induced changes in protein folding, stability, and dynamics.

Key Features:

• Experimental entries: Contains 14,669 experimental entries detailing thermodynamic parameters for both wild-type and mutant proteins, representing an 83% increase in unique mutation data compared to previous databases.
• Novel protein coverage: Includes thermodynamic information for 204 previously uncharacterized proteins.
• Thermodynamic parameters: Records changes in unfolding Gibbs free energy and melting temperature for individual mutations.
• Annotations and structural links: Provides detailed annotations for each entry and links entries to available experimental structural data.
• Manual curation: Entries have undergone rigorous manual curation with correction of annotation errors in previously curated records.
• Programmatic access: Offers access via a RESTful API for integration with computational workflows.
• Data submission: Accepts community-submitted experimental data points to expand the dataset.

Scientific Applications:

• Protein engineering: Enables selection and evaluation of mutations based on experimentally measured effects on stability for rational design and engineering strategies.
• Drug design: Supports assessment of mutation-induced stability changes that can affect target structure and ligand interactions.
• Molecular biology: Facilitates interpretation of how amino acid substitutions impact protein folding, stability, and function.
• Predictive modeling and benchmarking: Serves as a dataset for developing and benchmarking computational models that predict stability changes upon mutation.

Methodology:

Entries were compiled and subjected to rigorous manual curation with corrections of annotation errors; entries are linked to available experimental structural data and exposed via a RESTful API for programmatic access.