title: ProTherm, version 4.0: thermodynamic database for proteins and mutants.
abstract: Release 4.0 of ProTherm, thermodynamic database for proteins and mutants, contains approximately 14,500 numerical data (approximately 450% of the first version) of several thermodynamic parameters along with experimental methods and conditions, and structural, functional and literature information. The sequence and structural information of proteins is connected with thermodynamic data through links between entries in Protein Data Bank, Protein Information Resource and SWISS-PROT and the data in ProTherm. We have separated the Gibbs free energy change obtained at extrapolated temperature from the data on denaturation temperature measured by the thermal denaturation method. We have added the statistics of amino acid replacements and links to homologous structures to each protein. Further, we have improved the search and display options to enhance search capability through the web interface. ProTherm is freely available at http://gibk26. bse.kyutech.ac.jp/jouhou/Protherm/protherm.html.
authors.affiliation: Department of Biochemical Engineering and Science, Kyushu Institute of Technology (KIT), 680-4 Kawazu, Iizuka, 820-8502, Japan.
authors.forename: K Abdulla
authors.initials: KA
authors.lastname: Bava
authors.forename: M Michael
authors.initials: MM
authors.lastname: Gromiha
authors.forename: Hatsuho
authors.initials: H
authors.lastname: Uedaira
authors.forename: Koji
authors.initials: K
authors.lastname: Kitajima
authors.forename: Akinori
authors.initials: A
authors.lastname: Sarai
mesh_terms: D000818:Animals; D030562:Databases, Protein; D006801:Humans; D020407:Internet; D009154:Mutation / Q000235:genetics*; D011506:Proteins / Q000737:chemistry* / Q000235:genetics*; D013329:Structure-Activity Relationship; D013696:Temperature; D013816:Thermodynamics
chemical_list: D011506:Proteins