Saved in:
| Main Author: | |
|---|---|
| Format: | Recurso digital |
| Language: | |
| Published: |
Zenodo
2026
|
| Online Access: | https://doi.org/10.5281/zenodo.18950168 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Table of Contents:
- <h1><span lang="en-GB">Abstract</span></h1> <p><span lang="en-GB">We formulate the hypothesis that </span><span lang="en-GB"><strong>Z₁₂₀ = Z₃ × Z₅ × Z₈</strong></span><span lang="en-GB"> is a universal invariant of biological timing. The three factors have independent biological origins: Z₃ from the rotary mechanism of ATP synthase (Boyer 1997), Z₅ from the five substages of meiotic prophase I and from the cardinal identity |Z₁₆ \ {e}| = 15 = 3×5, and Z₈ from the Bott periodicity residue in the Clifford tower Cl⁺(3). Their product 120 = 3×5×8 appears simultaneously as: (i) the denominator of the spectral invariant </span>η<span lang="en-GB"> = 49/120 of the Dirac operator on T²/Z₁₆; (ii) the lifespan in days of the erythrocyte; (iii) the number of degrees in each step of the ATP synthase </span>γ<span lang="en-GB">-rotation; (iv) the period of the Rule 150/105 cellular automaton on a ring of size N=120. The hypothesis predicts that biological processes governed by Z₃ symmetry will manifest characteristic timescales that are multiples of 40 = lcm(8,5) = 120/3. We identify the collagen triple helix as the critical test case and propose a falsifiable research program.</span></p> <p lang="en-GB"> </p> <p><span lang="en-GB"><strong>Keywords: </strong></span><span lang="en-GB">Z₁₂₀, biological periodicity, ATP synthase, erythrocyte, spectral invariant, T144, orbifold, Clifford algebra, universality hypothesis</span></p>