RT Journal Article
SR Electronic
T1 High-quality thermodynamic data on the stability changes of proteins upon single-site mutations
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 036301
DO 10.1101/036301
A1 Fabrizio Pucci
A1 Raphaël Bourgeas
A1 Marianne Rooman
YR 2016
UL http://biorxiv.org/content/early/2016/01/10/036301.abstract
AB 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.