The first release of the Thermodynamic Database for Proteins and Mutants (P
roTherm) contains more than 3300 data of several thermodynamic parameters f
or wild type and mutant proteins. Each entry includes numerical data for un
folding Gibbs free energy change, enthalpy change, heat capacity change, tr
ansition temperature, activity etc., which are important for understanding
the mechanism of protein stability, ProTherm also includes structural infor
mation such as secondary structure and solvent accessibility of wild type r
esidues, and experimental methods and other conditions. A WWW interface ena
bles users to search data based on various conditions with different sortin
g options for outputs. Further, ProTherm is cross-linked with NCBI PUBMED l
iterature database, Protein Mutant Database, Enzyme Code and Protein Data B
ank structural database. Moreover, all the mutation sites associated with e
ach PDB structure are automatically mapped and can be directly viewed throu
gh 3DinSight developed in our laboratory, The database is available at the
URL, http://www.rtc. riken.go.jp/protherm.html.