Macroscopic Vibronic Coherence and Non-Dispersive Soliton Propagation Across a Protein-Solvent Interface

A foundational tenet of modern biophysics dictates that protein-solvent interactions and charge-transport dynamics operate strictly within microscopic, sub-nanometer boundaries where long-range coordination is natively suppressed by rapid room-temperature thermal dephasing. Here, we report an unexpected phenomenon that fundamentally challenges this paradigm: the long-distance, quantum-coherent communication between isolated protein samples in aqueous solution across macroscopic spatial separations. By mapping the distance-dependence of a weak, protein-emitted electromagnetic field on the response dynamics of an adjacent complex, we demonstrate that this inter-protein communication establishes a stable, intermolecular vibronic coupling operating across millimeter-scale distances up to at least 40 mm. This field interference induces a robust quantum coherence that lowers the local potential energy surface, transforming the coupled protein-solvent network into an un-attenuated, low-barrier energy transfer conduit. This stabilized pathway launches a topologically protected, non-dispersive soliton that exhibits exceptional phase stability against room-temperature thermal dephasing. These findings provide definitive empirical evidence of a sophisticated, field-driven quantum infrastructure embedded within a biological macromolecule. More explicitly, they reveal that a protein can possess an inherent capacity to preserve coherent wave propagation over macroscopic scales previously deemed impossible in room-temperature aqueous environments.