摘要

We investigated the field-dependent magnetic properties of chiral alanine crystals, especially associated with the electronic orbital motions. Based on the chirality of the zwitterionic model (+NH3- C(CH3) H-CO2-) and the helicity of the lattice structure of peptide bond in proteins, when an external field of +5 T was applied parallel to the preferred axis c(z) of the N+H center dot center dot center dot O- hydrogen bond in D-alanine, the electron spin-flip manifested emergent paramagnetism at 297.6 K. Because the spin magnetic dipole moment of hydrogen in L-alanine was originally aligned antiparallel to the field, the electron spins flipped firstly perpendicular to the field then manifested paramagnetism at 303.9 K. The magnetic field of 5 T split a degenerate energy level in the paramagnetic state of chiral alanine. Furthermore, the spin-orbital separation of the quasi-one dimensional N+H center dot center dot center dot O- hydrogen bond in the crystal lattice provided evidence for the hallmark of one-dimensional physics.

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