Protherm, version 4.0: thermodynamic database for proteins and mutants. 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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References in zbMATH (referenced in 3 articles )
Showing results 1 to 3 of 3.
- Miyazawa, Sanzo: Selection maintaining protein stability at equilibrium (2016)
- Ruiz-Blanco, Yasser B.; Marrero-Ponce, Yovani; Paz, Waldo; García, Yamila; Salgado, Jesús: Global stability of protein folding from an empirical free energy function (2013)
- Saraboji, K.; Gromiha, M.Michael; Ponnuswamy, M.N.: Relative importance of secondary structure and solvent accessibility to the stability of protein mutants. A case study with amino acid properties and energetics on T4 and human lysozymes (2005)