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The discovery of amino acids in meteorites has presented two clues to the origin of their processing subsequent to their formation: a slight preference for left-handedness in some of them, and isotopic anomalies in some of their constituent atoms. In this article we present theoretical results from the Supernova Neutrino Amino Acid Processing (SNAAP) model, which uses electron anti-neutrinos and the magnetic fields from source objects such as supernovae or colliding neutron stars to selectively destroy one amino acid chirality and to create isotopic abundance shifts. For plausible magnetic fields and electron anti-neutrino fluxes, non-zero, positive enantiomeric excesses, $ee$s, defined to be the relative left/right asymmetry in an amino acid population, are reviewed for two amino acids, and conditions are suggested that would produce $ee>0$ for all of the $alpha$-amino acids. The relatively high energy anti-neutrinos that produce the $ee$s would inevitably also produce isotopic anomalies. A nuclear reaction network was developed to describe the reactions resulting from them and the nuclides in the meteorites. At similar anti-neutrino fluxes, assumed recombination of the detritus from the anti-neutrino interactions is shown to produce appreciable isotopic anomalies in qualitative agreement with those observed for D/$^1$H and $^{15}$N/$^{14}$N. The isotopic anomalies for $^{13}$C/$^{12}$C are predicted to be small, as are also observed. Autocatalysis may be necessary for any model to produce the largest $ee$s observed in meteorites. This allows the constraints of the original SNAAP model to be relaxed, increasing the probability of meteoroid survival in sites where amino acid processing is possible. These results have obvious implications for the origin of life on Earth.
Magnetochiral phenomena may be responsible for the selection of chiral states of biomolecules in meteoric environments. For example, the Supernova Amino Acid Processing (SNAAP) Model was proposed previously as a possible mode of magnetochiral selecti
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A two amino acid (hydrophobic and polar) scheme is used to perform the design on target conformations corresponding to the native states of twenty single chain proteins. Strikingly, the percentage of successful identification of the nature of the res
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