Chirality of electrons from beta-decay and the left-handed asymmetry of proteins.

A simplified mathematical model of the origin of the left-handed asymmetry of proteins in living matter is presented. The model is based on the hypothesis of Vester and Ulbricht that the chirality of (left-handed) electrons from naturally beta-active elements, e.g. 14C, 40K, etc., was the specific source of the asymmetry; it requires for its application data on interaction of electrons having non-zero chirality with racemic mixtures of amino acids. This interaction is here treated theoretically in an order-of-magnitude calculation. Our analysis yields a very approximate value of the induced steady-state asymmetry in the amino acids at the beginning of protein synthesis and indicates that this asymmetry, though small, may have been sufficient to account for the dominant left-handedness of proteins now observed.