The electroweak origin of biomolecular handedness

Abstract

The parity-violating weak neutral current perturbation of the ground-state electronic energy has been calculated by ab initio methods for glycine over a range of chiral conformations, for L-alanine, L-α-aminopropionitrile, and for the peptide residue of polypeptides in the α-helix and the β-sheet conformation. It is found that L-alanine in its preferred conformation in aqueous solution and the L-peptides in the α-helix and the β-sheet conformation, have a lower ground-state energy than the corresponding D-enantiomers, because of the electroweak interaction. The enantiomer energy difference is small, of the order of 10 -14 J mol -1 , corresponding to an enantiomeric excess of 10 6 molecules of L-alanine or the L-peptide in one mole of the corresponding racemic mixture in thermodynamic equilibrium at ambient temperature. The significance of the energy difference between enantiomers arising from the electroweak interaction for the transition from racemic geochemistry to homochiral biochemistry in terrestrial evolution is discussed.