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Investigates signaling in neural tryptophan networks, suggesting a novel communication mechanism.
Building on recent evidence that dense Tryptophan (Trp) networks in protein lattices support room-temperature superradiance and ultrafast optical emission, we investigate the hypothesis that these emissions may serve a signaling function. Analysis of 20 cryo-EM and X-ray structures from the Protein Data Bank confirms that neural receptor and channel proteins contain 3–27 Trp residues with 1–28 quantum-coupled pairs (< 1.5 nm separation). We show that free-space radiative Trp-to-Trp energy transfer is physically impossible (p ≈ 1.8 × 10^-5), implying that if biophotons mediate inter-core communication, they must do so via an information channel rather than energy transfer. Switching to Cytochrome-c Oxidase (CCO) targets raises the per-core probability to p = 7.84 × 10^-4, and a parallel array of synchronized cores would achieve > 98% gating reliability via repetition coding over an asymmetric binary channel with zero false positives, should the proposed mechanism operate in vivo. The Trp–CCO Channel hypothesis operates at the quantum-to-classical boundary: quantum superradiance enables efficient photon generation, while classical information theory governs the signaling. Energy per bit is ~6.23 × 10^5 times the Landauer limit, ~16-fold more efficient than classical CMOS and consuming < 2% of the brain's 20 W budget at rest. This framework is testable via superradiance scaling and phase-interference experiments
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Kumar et al. (2026) studied this question.
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