This research proposes a new quasiparticle to explain long-range oscillations in crystalline proteins, suggesting a novel understanding of coherence.
Long-range, underdamped collective oscillations in the 0.1–2.0 THz window have been observedin crystalline proteins by optical near-field spectroscopy, but their physical mechanism has remainedunexplained: conventional normal-mode analysis predicts stronger damping and shorter coherence lengthsthan are measured. We propose that these oscillations are the experimental signature of the organizon—themassive amplitude excitation of a scalar coherence field whose minimal polynomial Lagrangian is selectedby three structural conditions (kinetic coupling, conservation law, bounded dynamics). At the topologicalboundary κ = 0 the effective potential belongs to the tricritical universality class with order-parameterexponent β = 1/4, which (i) suppresses inter-mode coupling and explains the anomalously weak damping,and (ii) yields three exponent-level falsifiable predictions (no adjustable critical exponents) accessiblewith existing THz instrumentation: P1 the THz oscillation amplitude scales as ATHz ∝ (ρ_eff − ρ_c)1/4under controlled dehydration; P2 the integrated THz spectral weight undergoes a logistic transition as afunction of hydration level, with inflection at the half-condensation point C∗ = 0.5; P3 the damping rateΓ(ρ_eff) passes through a minimum near ρc as inter-mode coupling is suppressed by tricritical curvature.Prediction P1 distinguishes the organizon picture from all conventional phonon or normal-mode models,which yield β = 1/2 or Ising-class exponents. The inverse scaling law Φc ∝ ρ_eff^-1 , previously validated against protein denaturation data (R2 = 0.975, eight SCOP classes), is rederived here as a consequence ofthe same Lagrangian, establishing internal consistency of the framework
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Jonah Y. C. Hsu (2026) studied this question.
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