Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring

Jeffrey M. Dick, Everett Shock

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Uncovering the chemical and physical links between natural environments and microbial communities is becoming increasingly amenable owing to geochemical observations and metagenomic sequencing. At the hot spring known as Bison Pool in Yellowstone National Park, the cooling of the water in the outflow channel is associated with an increase in oxidation potential estimated from multiple field-based measurements. Representative groups of proteins whose sequences were derived from metagenomic data also exhibit an increase in average oxidation state of carbon in the protein molecules with distance from the hot-spring source. The energetic requirements of reactions to form selected proteins used in the model were computed using amino-acid group additivity for the standard molal thermodynamic properties of the proteins, and the relative chemical stabilities of the proteins were investigated by varying temperature, pH and oxidation state, expressed as activity of dissolved hydrogen. The relative stabilities of the proteins were found to track the locations of the sampling sites when the calculations included a function for hydrogen activity that increases with temperature and is higher, or more reducing, than values consistent with measurements of dissolved oxygen, sulfide and oxidation-reduction potential in the field. These findings imply that spatial patterns in the amino acid compositions of proteins can be linked, through energetics of overall chemical reactions representing the formation of the proteins, to the environmental conditions at this hot spring, even if microbial cells maintain considerably different internal conditions. Further applications of the thermodynamic calculations are possible for other natural microbial ecosystems.

Original languageEnglish (US)
Article numbere22782
JournalPLoS One
Volume6
Issue number8
DOIs
StatePublished - 2011

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Hot springs
Hot Springs
hot springs
Protein Stability
Chemical stability
Oxidation-Reduction
chemistry
Temperature
Metagenomics
temperature
Proteins
proteins
Thermodynamics
oxidation
Hydrogen
thermodynamics
hydrogen
Bison
Oxidation
Amino Acids

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring. / Dick, Jeffrey M.; Shock, Everett.

In: PLoS One, Vol. 6, No. 8, e22782, 2011.

Research output: Contribution to journalArticle

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