Mechanically modulated spin orbit couplings in oligopeptides

TL;DR

This paper develops an analytical model for spin-orbit interactions in oligopeptides, revealing how molecular deformations influence spin activity, consistent with recent experimental findings on biological molecules.

Contribution

It introduces a tight-binding Hamiltonian model incorporating intrinsic and Rashba spin-orbit interactions in oligopeptides, highlighting deformation effects on spin activity.

Findings

SO strengths in the tens of meV range

Deformation potentials can enhance or diminish SO strength

Qualitative agreement with recent experimental observations

Abstract

Recently experiments have shown very significant spin activity in biological molecules such as DNA, proteins, oligopeptides and aminoacids. Such molecules have in common their chiral structure, time reversal symmetry and the absence of magnetic exchange interactions. The spin activity is then assumed to be due to either the pure Spin-orbit (SO) interaction or SO coupled to the presence of strong local sources of electric fields. Here we derive an analytical tight-binding Hamiltonian model for Oligopeptides that contemplates both intrinsic SO and Rashba interaction induced by hydrogen bond. We use a lowest order perturbation theory band folding scheme and derive the reciprocal space intrinsic and Rashba type Hamiltonian terms to evaluate the spin activity of the oligopeptide and its dependence of molecule uniaxial deformations. SO strengths in the tens of meV are found and explicit spin active deformation potentials. We find a rich interplay between responses to deformations both to enhance and diminish SO strength that allow for experimental testing of the orbital model. Qualitative consistency with recent experiments shows the role of hydrogen bonding in spin activity.