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ProTherm, version 4.0: thermodynamic database for proteins and mutants
Author(s) -
K. Abdulla Bava,
M. Michael Gromiha,
Hatsuho Uedaira,
K. Kitajima,
Akinori Sarai
Publication year - 2003
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/gkh082
Subject(s) - protein data bank , biology , gibbs free energy , denaturation (fissile materials) , interface (matter) , mutant , database , process (computing) , protein structure , computational biology , data mining , thermodynamics , biochemistry , computer science , physics , gene , pulmonary surfactant , gibbs isotherm , nuclear physics , operating system
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.

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