Go to the abstract in the NAR 2002 Database Issue.
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Contact gromiha@rtc.riken.go.jp
Thermodynamic database for proteins and mutants (ProTherm) is a collection of numerical data for several thermodynamic parameters, such as, unfolding Gibbs free energy change, enthaply change, heat capacity change, transition temperature and activity, which are important for understanding the mechanism of protein stability. ProTherm also includes experimental methods and conditions, reversibility of folding, details about the surrounding residues in space for all mutants, structural, functional and literature information. The current release contains more than 7100 entries, an ~115% increase over the first version. In addition, we have included information about the source of each protein, protein concentration and identification codes for SWISS-PROT and Protein Information Resource. A WWW interface enables users to search data based on various conditions with different sorting options for outputs. Further, ProTherm is cross-linked with Protein Data Bank, Protein Mutant Database, Enzyme code, BRENDA and PUBMED literature database. Moreover, the mutation sites and surrounding residues are automatically mapped on the structure and can be directly viewed through 3DinSight developed in our laboratory. The ProTherm database is freely available at http://www.rtc.riken.go.jp/jouhou/protherm/protherm.html.
Category Structure
Go to the abstract in the NAR 2002 Database Issue.