Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250 °C

  title={Hydrolytic stability of biomolecules at high temperatures and its implication for life at 250 °C},
  author={Robert H White},
The upper temperature at which a living system can exist is limited by the hydrolytic breakdown rate of its chemical constituents. The peptide bonds of proteins, the phosphodiester and N-glycosyl bonds in RNA and DNA, and the pyrophosphate and N-glycosyl bonds in nucleotides such as ATP and NAD are among the more important bonds that will undergo hydrolysis. The decomposition of biomolecules via non-hydrolytic pathways such as decarboxylations and dehydrations may also be critical factors in… Expand
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  • Chemistry, Medicine
  • Advances in space research : the official journal of the Committee on Space Research
  • 1986
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Quantitative studies of the effect of some metal ions on the reaction of glycyl-glycine (gg) in the pH ranges 0.3–1.0 and 3.8–6.0 and temperatures ranging from 364 to 387 K are reported. In the pHExpand
Irreversible heat inactivation of transfer ribonucleic acids.
  • T. Lindahl
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 1967
Whereas depurination, deamination, and aggregation have been ruled out as additional important means of heat inactivation in the absence of Mg++, the destruction of 5,6-dihydrouridylic acid residues appears to be a quantitatively significant one. Expand
Thermophilic Microorganisms and Life at High Temperatures
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Previous racemization and epimerization studies with dipeptides have not taken into account the formation of diketopiperazines and, as a result, the cortclusions about the mechanism and geochemical implications of amino acid racemizes will require revision. Expand
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