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A collection of numerical data of thermodynamic parameters such as Gibbs free energy change, enthalpy change, heat capacity change, transition temperature etc. for wild type and mutant proteins that are important for understanding the structure and stability of proteins. It also contains information about secondary structure and accessibility of wild type residues, experimental conditions (pH, temperature, buffer, ion and protein concentration), measurements and methods used for each data, and activity information (Km and Kcat).


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Provides unbiased training and validation datasets for the development of algorithms to predict binding affinity changes due to missense mutations. The PROXiMATE database helps about the study of disease-causing mutations in the progression, diagnosis and treatment of various diseases. It gives possible drug targets and novel therapy options. More, it supplies experimental data for the identification of mutants which show increased affinity to their interacting partners.