We have set up and manually curated a dataset containing experimental information on the impact of amino acid substitutions in a protein on its thermal stability. It consists of a repository of experimentally measured melting temperatures (Tm) and their changes upon point mutations (ΔTm) for proteins having a well-resolved x-ray structure. This high-quality dataset is designed for being used for the training or benchmarking of in silico thermal stability prediction methods. It also reports other experimentally measured thermodynamic quantities when available, i.e., the folding enthalpy (ΔH) and heat capacity (ΔCP) of the wild type proteins and their changes upon mutations (ΔΔH and ΔΔCP), as well as the change in folding free energy (ΔΔG) at a reference temperature. These data are analyzed in view of improving our insights into the correlation between thermal and thermodynamic stabilities, the asymmetry between the number of stabilizing and destabilizing mutations, and the difference in stabilization potential of thermostable versus mesostable proteins.
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June 2016
Research Article|
June 03 2016
High-quality Thermodynamic Data on the Stability Changes of Proteins Upon Single-site Mutations Available to Purchase
Fabrizio Pucci;
Fabrizio Pucci
a)
Department of BioModeling, BioInformatics and BioProcesses,
Université Libre de Bruxelles
, CP 165/61, Roosevelt Avenue 50, 1050 Brussels, Belgium
and Interuniversity Institute of Bioinformatics in Brussels
, CP 263, Triumph Bld, 1050 Brussels, Belgium
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Raphaël Bourgeas;
Raphaël Bourgeas
b)
Department of BioModeling, BioInformatics and BioProcesses,
Université Libre de Bruxelles
, CP 165/61, Roosevelt Avenue 50, 1050 Brussels, Belgium
and Interuniversity Institute of Bioinformatics in Brussels
, CP 263, Triumph Bld, 1050 Brussels, Belgium
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Marianne Rooman
Marianne Rooman
c)
Department of BioModeling, BioInformatics and BioProcesses,
Université Libre de Bruxelles
, CP 165/61, Roosevelt Avenue 50, 1050 Brussels, Belgium
and Interuniversity Institute of Bioinformatics in Brussels
, CP 263, Triumph Bld, 1050 Brussels, Belgium
Search for other works by this author on:
Fabrizio Pucci
a)
Raphaël Bourgeas
b)
Marianne Rooman
c)
Department of BioModeling, BioInformatics and BioProcesses,
Université Libre de Bruxelles
, CP 165/61, Roosevelt Avenue 50, 1050 Brussels, Belgium
and Interuniversity Institute of Bioinformatics in Brussels
, CP 263, Triumph Bld, 1050 Brussels, Belgium
a)
Electronic mail: [email protected].
b)
Electronic mail: [email protected].
c)
Electronic mail: [email protected].
J. Phys. Chem. Ref. Data 45, 023104 (2016)
Article history
Received:
January 08 2016
Accepted:
April 12 2016
Citation
Fabrizio Pucci, Raphaël Bourgeas, Marianne Rooman; High-quality Thermodynamic Data on the Stability Changes of Proteins Upon Single-site Mutations. J. Phys. Chem. Ref. Data 1 June 2016; 45 (2): 023104. https://doi.org/10.1063/1.4947493
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