Stability of peptides in high-temperature aqueous solutions

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

Estimated standard molal thermodynamic properties of aqueous dipeptides and their constituent amino acids indicate that temperature increases correspond to increased stability of peptide bonds relative to hydrolysis reactions. Pressure increases cause slight decreases in peptide bond stability, which are generally offset by greater stability caused by temperature increases along geothermal gradients. These calculations suggest that peptides, polypeptides, and proteins may survive hydrothermal alteration of organic matter depending on the rates of the hydrolysis reactions. Extremely thermophilic organisms may be able to take advantage of the decreased energy required to form peptide bonds in order to maintain structural proteins and enzymes at elevated temperatures and pressures. As the rates of hydrolysis reactions increase with increasing temperature, formation of peptide bonds may become a facile process in hydrothermal systems and deep in sedimentary basins.

Original languageEnglish (US)
Pages (from-to)3481-3491
Number of pages11
JournalGeochimica et Cosmochimica Acta
Volume56
Issue number9
DOIs
StatePublished - 1992
Externally publishedYes

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peptide
aqueous solution
Peptides
hydrolysis
Hydrolysis
Temperature
temperature
protein
thermodynamic property
geothermal gradient
hydrothermal system
hydrothermal alteration
Dipeptides
sedimentary basin
Biological materials
amino acid
enzyme
Proteins
Thermodynamic properties
organic matter

ASJC Scopus subject areas

  • Geochemistry and Petrology

Cite this

Stability of peptides in high-temperature aqueous solutions. / Shock, Everett.

In: Geochimica et Cosmochimica Acta, Vol. 56, No. 9, 1992, p. 3481-3491.

Research output: Contribution to journalArticle

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