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. 2004 Jan 1;32(Database issue):D120-1.
doi: 10.1093/nar/gkh082.

ProTherm, version 4.0: thermodynamic database for proteins and mutants

K Abdulla Bava  1 , M Michael Gromiha, Hatsuho Uedaira, Koji Kitajima, Akinori Sarai
Affiliations

ProTherm, version 4.0: thermodynamic database for proteins and mutants

K Abdulla Bava et al. Nucleic Acids Res. .

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.

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Figures

Figure 1
Figure 1
Growth of ProTherm: (a) total numbers of entries and mutations; (b) numbers of all proteins and references.
Figure 1
Figure 1
Growth of ProTherm: (a) total numbers of entries and mutations; (b) numbers of all proteins and references.
See this image and copyright information in PMC

References

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    1. Gromiha M.M., Uedaira,H., An,J., Selvaraj,S., Prabakaran,P. and Sarai,A. (2002) ProTherm, thermodynamic database for proteins and mutants: developments in version 3.0. Nucleic Acids Res., 30, 301–302. - PMC - PubMed
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