Abstract
Thermodynamic data for proteins are important for understanding the mechanism of protein stability. Pfeil [1] collected a set of thermodynamic data on protein folding and stability from experimental studies. Recently, we have developed an electronically accessible Thermodynamic Database for Proteins and Mutants (ProTherm) [2], which includes several thermodynamic data (unfolding Gibbs free energy change, enthalpy change, heat capacity change, transition temperature, activity, etc.), structural information (secondary structure, solvent accessibility, etc.), measuring methods, experimental conditions and literature information. We have developed a WWW interface to facilitate searching the database and sorting outputs. At present, the number of data has been increased to more than 5,500 covering the latest experimental data and several new features have been included in the database.
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