Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry 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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Autores principales:	Jeffrey M Dick, Everett L Shock
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3aa74be57e1a496ba97451e5e4432d83
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spelling	oai:doaj.org-article:3aa74be57e1a496ba97451e5e4432d832021-11-18T06:48:12ZCalculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.1932-620310.1371/journal.pone.0022782https://doaj.org/article/3aa74be57e1a496ba97451e5e4432d832011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21853048/?tool=EBIhttps://doaj.org/toc/1932-6203Uncovering 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.Jeffrey M DickEverett L ShockPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 8, p e22782 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jeffrey M Dick Everett L Shock Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
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 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.
format	article
author	Jeffrey M Dick Everett L Shock
author_facet	Jeffrey M Dick Everett L Shock
author_sort	Jeffrey M Dick
title	Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
title_short	Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
title_full	Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
title_fullStr	Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
title_full_unstemmed	Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
title_sort	calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/3aa74be57e1a496ba97451e5e4432d83
work_keys_str_mv	AT jeffreymdick calculationoftherelativechemicalstabilitiesofproteinsasafunctionoftemperatureandredoxchemistryinahotspring AT everettlshock calculationoftherelativechemicalstabilitiesofproteinsasafunctionoftemperatureandredoxchemistryinahotspring
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Calculation of the relative chemical stabilities of proteins as a function of temperature and redox chemistry in a hot spring.

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