Amino acid racemization dating desperate women dating
Amino acids have been reported from fossils distributed throughout the geologic column (Florkin 1969).Since detectable levels of many amino acids are expected to survive only a few million years, at best, these observations are an enigma (Abelson 1956, 1957).Figure 2 illustrates this pattern for isoleucine, which together with aspartic acid has received the greatest attention in amino acid dating. The racemic mixture resulting from the epimerization of isoleucine has been determined to have a ratio of D-alloisoleucine to L-isoleucine in the range 1.25/1 to 1.4/1, with greatest confidence in a figure near 1.25/1.Interaction among diastereomers is called epimerization. For comparison of work done by different investigators 1.25/1 is accepted as a standard value (Kvenvolden 1975, Bada 1981, Wehmiller and Belknap 1982).Investigation of amino acids in fossils over the past thirty years has revealed that residual amino acids may exist in fossils from throughout the Phanerozoic portion of the geologic column, that the amino acid pattern in a given fossil changes with age due to differences in stability among the twenty amino acids of which proteins are constructed, and that the ratio of right-handed to left-handed forms (D/L ratio) of amino acids increases with age from zero in the proteins of living organisms to the ratios which are characteristic of amino acids produced synthetically (the racemic ratios).
All other physical properties of the L- and D-forms of a given amino acid are identical, and of course the chemical compositions are identical.The coefficient of t is presumed to be a constant, corresponding to m, and Const. Since the D-form does not exist in the amino acids of proteins in living organisms, the logarithmic term for t = 0 should be zero (ln 1 = 0), which specifies a zero value for Const.A non-zero constant term may be required to adjust for a slight racemization produced during the laboratory preparation of a sample (Bada and Shou 1980).Four of the amino acids that make up proteins isoleucine, threonine, hydroxyproline, and hydroxylysine have two asymmetric carbon atoms which produce four structural possibilities for the same chemical composition.Two of these forms are designated as diastereomers, each of which may exist in either an L- or a D-form.