Abstract
ONE of the most intriguing problems in chemical evolution is the origin of optical asymmetry in biopolymers. The easiest way to state the problem is: why are proteins made almost exclusively of L-amino acid optical isomers and natural sugars of D-optical isomers?1 That proteins must be made of only one kind of optical isomer is understandable on the basis of their need for precise three-dimensional conformations in order to perform their catalytic roles as enzymes. But, is it just a matter of chance, as suggested in refs 2–4, that our proteins are L-, or is there (was there) some asymmetrical agent on our planet that made the protein L-configuration the one upon which life is based?
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LEMMON, R., CROWE, K., GYGAX, F. et al. Search for selectivity between optical isomers in reactions of polarised positive muons with alanines and octanols. Nature 252, 692–694 (1974). https://doi.org/10.1038/252692a0
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DOI: https://doi.org/10.1038/252692a0
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