Phase diagram of a semiflexible magnetic polymer in three dimensions

Abstract

We study a semiflexible magnetic polymer in which each monomer carries a two-state spin, giving rise to coupled conformational, stiffness, and magnetic degrees of freedom. The model provides a minimal representation of nucleoprotein complexes in vivo, in which DNA bending rigidity and bridging proteins must be simultaneously accommodated. We employ Monte Carlo simulations on a face-centered-cubic (FCC) lattice, complemented by a variational free-energy upper-bound approach, to characterize the zero-field phase diagram as a function of bending stiffness and temperature. At low stiffness, we identify a first-order transition combining coil-to-globule collapse with a ferromagnetic-to-paramagnetic transition. At lower temperatures, an additional first-order transition separates the disordered globule from an ordered crystal characterized by nematic-like orientational order of the bond tangents. At high stiffness, the globule disappears, resulting in a direct first-order coil-to-crystal transition. These results demonstrate how chain stiffness and magnetic degrees of freedom couple to polymer conformation and reorganize the zero-field phase diagram. Our model connects the two limiting cases of flexible magnetic polymers and semiflexible homopolymers, the latter corresponding to the strong-field limit in which all spins are aligned.