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Biomaterials are primarily insulators. For nearly a century, electromagnetic resonance and antenna–receiver properties have been measured and extensively theoretically modeled. The dielectric constituents of biomaterials—if arranged in distinct symmetries, then each vibrational symmetry—would lead to a distinct resonance frequency. While the literature is rich with data on the dielectric resonance of proteins, scale-free relationships of vibrational modes are scarce. Here, we report a self-similar triplet of triplet resonance frequency pattern for the four-4 nm-wide tubulin protein, for the 25-nm-wide microtubule nanowire and 1-μm-wide axon initial segment of a neuron. Thus, preserving the symmetry of vibrations was a fundamental integration feature of the three materials. There was no self-similarity in the physical appearance: the size varied by 106 orders, yet, when they vibrated, the ratios of the frequencies changed in such a way that each of the three resonance frequency bands held three more bands inside (triplet of triplet). This suggests that instead of symmetry, self-similarity lies in the principles of symmetry-breaking. This is why three elements, a protein, it’s complex and neuron resonated in 106 orders of different time domains, yet their vibrational frequencies grouped similarly. Our work supports already-existing hypotheses for the scale-free information integration in the brain from molecular scale to the cognition.

Fractal, Scale Free Electromagnetic Resonance of a Single Brain Extracted Microtubule Nanowire, a Single Tubulin Protein and a Single Neuron