Exchanged flying ring of homochiral bosonic field in the genetic code.

We present the proof for the source of exchange flying ring of the biological bosonic state in homochirality of L-amino acids. It is a source of knot in parallel transport of Yang–Mills field in genetic code evolved from natural selection. It serves as a source of protein folding structure in L-amino acids over all the protein structure of a living organism. In the proof, we modified Frank's model for homochirality and added more properties of nonlinearity and supersymmetry. The mirror symmetries transform their left and right homochiral hidden states of reversed reaction over Frank's equation for spontaneous autocatalysis. We also change the rate of reaction in the model from the Euclidean norm to Minkowski metric with Lorentz invariant in special relativity theory. The speed of light in Minkowski space in this model is an analogy with a source of all species of all living organisms with common 20 L-amino acids as their constituents. The result of the proof agrees with the existence of L-amino acids in nature. By long-term of evolution, the number of concentration of left homochirality is more than the concentration of right homochirality in amino acids propositional to the Chern–Simons current. [ABSTRACT FROM AUTHOR]