Recent Developments in ProTherm: Thermodynamic Database for Proteins and Mutants
نویسندگان
چکیده
Due to the rapid progress in genome analysis, complete genome sequences of many organisms become available. Now proteins are the next target for intensive study, as evidenced by the emerging fields such as structural genomics and proteome analysis. In order to elucidate molecular function of proteins, we need to have knowledge of their amino acid sequence and structure. The sequence and structural information, however, is not enough to infer the protein function, because protein is a microscopic entity and its behavior obeys the law of thermodynamics. Thus, the information of thermodynamic quantities of proteins and their interactions is as fundamental as sequence and structural information. Although the databases for sequence and structure are well established and available, databases for thermodynamic quantities on protein stability and interactions are few. Thermodynamic data for proteins are essential not only for understanding the mechanism of protein folding and stability, but also for designing stable mutants. The compilation of thermodynamic data along with the sequence, structural, functional and literature information would be a valuable resource for such studies [2, 4]. Thus, we have designed an electronically accessible database, ProTherm [3], including several thermodynamic parameters, along with sequence and structural information, experimental methods and conditions, and literature information. Further, we have provided a WWW interface to facilitate searching the database, sorting and visualizing the results. Currently ProTherm contains about 12,000 entries.
منابع مشابه
Recent Developments of ProTherm: Thermodynamic Database for Proteins and Mutants
Thermodynamic data for proteins are important for understanding the mechanism of protein folding and stability. In recent years, the accumulation of thermodynamic data has been steadily increasing. Pfeil [4] collected a set of thermodynamic data on protein folding and stability from experimental studies that have been published until 1996. Recently, we have developed an electronically accessibl...
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The first release of the Thermodynamic Database for Proteins and Mutants (ProTherm) contains more than 3300 data of several thermodynamic parameters for wild type and mutant proteins. Each entry includes numerical data for unfolding Gibbs free energy change, enthalpy change, heat capacity change, transition temperature, activity etc., which are important for understanding the mechanism of prote...
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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 ...
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Thermodynamic data for proteins are important for understanding the mechanism of protein stability. Pfeil [1] collected a set of thermodynamic data on protein folding and stability from experimental studies. Recently, we have developed an electronically accessible Thermodynamic Database for Proteins and Mutants (ProTherm) [2], which includes several thermodynamic data (unfolding Gibbs free ener...
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