|Title||High-quality thermodynamic data on the stability changes of proteins upon single-site mutations|
|Publication Type||Journal Article|
|Year of Publication||2016|
|Authors||Pucci, F, Bourgeas, R, Rooman, M|
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 (∆Tm) 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 (∆H) and heat capacity (∆CP) of the wild type proteins and their changes upon mutations (∆∆H and ∆∆CP ), as well as the change in folding free energy (∆∆G) 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.
High-quality thermodynamic data on the stability changes of proteins upon single-site mutations
Posted on Saturday, February 25, 2017