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PreprintCC BY 4.0arXiv

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.

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BibTeX
@misc{delimi2026phase,
  title = {{Phase diagram of a semiflexible magnetic polymer in three dimensions}},
  author = {Linda Delimi and Arpan Dey and Jean-Charles Walter},
  howpublished = {arXiv},
  year = {2026},
  month = oct,
  doi = {10.48550/arxiv.2610.08958},
  eprint = {2610.08958},
  archivePrefix = {arXiv},
  url = {https://arxiv.org/abs/2610.08958},
  note = {CC BY 4.0},
}
RIS
TY  - UNPB
TI  - Phase diagram of a semiflexible magnetic polymer in three dimensions
AU  - Linda Delimi
AU  - Arpan Dey
AU  - Jean-Charles Walter
PY  - 2026
DA  - 2026/10/06
PB  - arXiv
DO  - 10.48550/arxiv.2610.08958
UR  - https://arxiv.org/abs/2610.08958
AB  - 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.
ER  -