Abstract
It is a well established notion that animals can detect the Earth's magnetic field, while the biophysical origin of such magnetoreception is still elusive. Recently, a magnetic receptor Drosophila CG8198 (MagR) with a rodlike protein complex is reported [S. Qin et al., Nat. Mater. 15, 217 (2016)] to act like a compass needle to guide the magnetic orientation of animals. This view, however, is challenged [M. Meister, Elife 5, e17210 (2016)] by arguing that thermal fluctuations beat the Zeeman coupling of the proteins's magnetic moment with the rather weak geomagnetic field ( ). In this work, we show that the spin-mechanical interaction at the atomic scale gives rise to a high blocking temperature which allows a good alignment of the protein's magnetic moment with the Earth's magnetic field at room temperature. Our results provide a promising route to resolve the debate on the thermal behaviors of MagR, and may stimulate a broad interest in spin-mechanical couplings down to atomistic levels.
- Received 7 January 2018
DOI:https://doi.org/10.1103/PhysRevE.97.042409
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