Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring
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 outflo...
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| Format: | Journal Article |
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Public Library of Science
2011
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| Online Access: | http://hdl.handle.net/20.500.11937/16196 |
| _version_ | 1848749106403475456 |
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| author | Dick, Jeffrey Shock, E. |
| author_facet | Dick, Jeffrey Shock, E. |
| author_sort | Dick, Jeffrey |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | 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 usedin 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. |
| first_indexed | 2025-11-14T07:15:40Z |
| format | Journal Article |
| id | curtin-20.500.11937-16196 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T07:15:40Z |
| publishDate | 2011 |
| publisher | Public Library of Science |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-161962017-09-13T15:54:45Z Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring Dick, Jeffrey Shock, E. 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 usedin 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. 2011 Journal Article http://hdl.handle.net/20.500.11937/16196 10.1371/journal.pone.0022782 Public Library of Science fulltext |
| spellingShingle | Dick, Jeffrey Shock, E. Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title | Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title_full | Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title_fullStr | Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title_full_unstemmed | Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title_short | Calculation of the Relative Chemical Stabilities of Proteins as a Function of Temperature and RedoxChemistry in a Hot Spring |
| title_sort | calculation of the relative chemical stabilities of proteins as a function of temperature and redoxchemistry in a hot spring |
| url | http://hdl.handle.net/20.500.11937/16196 |