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Nucleic Acids Research, 2004, Vol. 32, Database issue D120-D121
© 2004 Oxford University Press

ProTherm, version 4.0: thermodynamic database for proteins and mutants

K. Abdulla Bava, M. Michael Gromiha1, Hatsuho Uedaira, Koji Kitajima and Akinori Sarai*

Department of Biochemical Engineering and Science, Kyushu Institute of Technology (KIT), 680–4 Kawazu, Iizuka, 820-8502, Japan and 1 Computational Biology Research Center (CBRC), National Institute of Advanced Industrial Science and Technology (AIST), 2–43 Aomi Frontier Building 17F, Koto-ku, Tokyo 135-0064, Japan

*To whom correspondence should be addressed. Tel: +81 948 29 7811, Fax: +81 948 29 7841; Email: sarai{at}bse.kyutech.ac.jp

Release 4.0 of ProTherm, thermodynamic database for proteins and mutants, contains ~14 500 numerical data (~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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