Jan 10, 2016

High-quality thermodynamic data on the stability changes of proteins upon single-site mutations

BioRxiv : the Preprint Server for Biology
Fabrizio PucciMarianne Rooman

Abstract

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.

  • References
  • Citations

References

  • We're still populating references for this paper, please check back later.
  • References
  • Citations

Citations

  • This paper may not have been cited yet.

Mentioned in this Paper

Chloropicrin
Plain X-ray
Staphylococcal Protein A
Site
Chemical Substitution
Structure
Radiographic Imaging Procedure
Enzyme Stability
Silo (Dataset)
Amino Acid Substitution

About this Paper

Related Feeds

BioRxiv & MedRxiv Preprints

BioRxiv and MedRxiv are the preprint servers for biology and health sciences respectively, operated by Cold Spring Harbor Laboratory. Here are the latest preprint articles (which are not peer-reviewed) from BioRxiv and MedRxiv.