Protein thermal stabilization by charged compatible solutes: Computational studies in rubredoxin from Desulfovibrio gigas

Research output: Contribution to journalArticlepeer-review

Abstract

Molecular dynamics simulation studies of rubredoxin from Desulfovibrio gigas (RDG) were used to characterize the molecular mechanism of thermal stabilization by the compatible solute (CS) diglycerol-phospate (DGP). DGP is a negatively charged CS that accumulates under salt stress in Archaeoglobus fulgidus. Experimental results show that a 100 mM DGP solution exerts a strong protection effect in the half-life of RDG at 363 K (Lamosa et al., Appl Environ Microbiol 2000;66: 1974-1979). RDG was simulated in four aqueous solutions at 300 and 363 K: pure aqueous media, 100 mM DGP, 100 mM NaCl, and 500 mM DGP. Our work shows that the 100 mM DGP solution is able to maintain the average protein structure when the temperature is increased, preventing the occurrence of large-scale deviation of a mobile loop involved in the first steps of RDG unfolding. The molecular mechanism of thermal denaturation protection by DGP seems to involve the direct interaction between the protein and the CS by hydrogen bond interactions near the mobile loop. Several clusters of DGP molecules are formed and preferentially localized at neutral electrostatic regions of the surface. The increase of DGP concentration to 500 mM did not yield better stabilization of the protein suggesting that the thermal protective role of this charged CS is achieved at low concentrations, as shown experimentally.

Original languageEnglish
Pages (from-to)580-588
Number of pages9
JournalProteins: Structure, Function and Genetics
Volume72
Issue number2
DOIs
Publication statusPublished - 1 Aug 2008

Keywords

  • Compatible solutes
  • Diglycerol-phosphate
  • Molecular dynamics simulation
  • Rubredoxin
  • Thermostability

Fingerprint Dive into the research topics of 'Protein thermal stabilization by charged compatible solutes: Computational studies in rubredoxin from Desulfovibrio gigas'. Together they form a unique fingerprint.

Cite this