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2025
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| Online Access: | https://doi.org/10.5281/zenodo.17102271 |
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| _version_ | 1866902208764706816 |
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| author | Washburn, Jonathan |
| author_facet | Washburn, Jonathan |
| contents | <p>A minimal recognition principle fixes a golden-ratio cascade rn = LP phi^n and a single coherence quantum Ecoh = 0.090 eV. With no tuned energetic parameters, this constant alone predicts B-DNA geometry and elasticity and the kinetics of RNA polymerases. The cascade selects the canonical minor-groove width (13.6 Angstroms) and helical pitch (34.6 Angstroms). A quadratic fluctuation expansion yields bending and twist persistence lengths A approximately 56 nm and C approximately 72 nm at physiological salt, matching experiment after standard electrostatic corrections. Polymerase translocation follows an integer-quantum gate: multi-subunit RNAPs use n* = 3 and T7 uses n* = 2, fixing activation energies and the Arrhenius slope. A drag-limited law then sets a hard ceiling near 50 bp s^-1 (E. coli) and reproduces stall forces (~14 pN multi-subunit; 25-30 pN T7) without altering Ecoh. Pausing emerges from fixed escape barriers 2Ecoh and 5/2 Ecoh, giving invariant lifetimes of ~1 s (elemental) and ~10 s (back-tracked) across enzymes; sequence only modulates entry via nascent-RNA hairpin Delta G. The framework collapses a historically empirical domain to a deterministic, audit-ready core: one universal quantum, integer gates, and benign per-enzyme drag/prefactor fits. It makes crisp, falsifiable predictions: (i) cross-enzyme force-velocity collapse in reduced units, (ii) 1/T scaling of A and C at fixed ionic strength, and (iii) a pump-probe sideband at 3Ecoh.</p> |
| format | Recurso digital |
| id | zenodo_https___doi_org_10_5281_zenodo_17102271 |
| institution | Zenodo |
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| publishDate | 2025 |
| publisher | Zenodo |
| record_format | zenodo |
| spellingShingle | Parameter-Free DNA Mechanics and Transcription Kinetics from a Single 0.090 eV Quantum Washburn, Jonathan <p>A minimal recognition principle fixes a golden-ratio cascade rn = LP phi^n and a single coherence quantum Ecoh = 0.090 eV. With no tuned energetic parameters, this constant alone predicts B-DNA geometry and elasticity and the kinetics of RNA polymerases. The cascade selects the canonical minor-groove width (13.6 Angstroms) and helical pitch (34.6 Angstroms). A quadratic fluctuation expansion yields bending and twist persistence lengths A approximately 56 nm and C approximately 72 nm at physiological salt, matching experiment after standard electrostatic corrections. Polymerase translocation follows an integer-quantum gate: multi-subunit RNAPs use n* = 3 and T7 uses n* = 2, fixing activation energies and the Arrhenius slope. A drag-limited law then sets a hard ceiling near 50 bp s^-1 (E. coli) and reproduces stall forces (~14 pN multi-subunit; 25-30 pN T7) without altering Ecoh. Pausing emerges from fixed escape barriers 2Ecoh and 5/2 Ecoh, giving invariant lifetimes of ~1 s (elemental) and ~10 s (back-tracked) across enzymes; sequence only modulates entry via nascent-RNA hairpin Delta G. The framework collapses a historically empirical domain to a deterministic, audit-ready core: one universal quantum, integer gates, and benign per-enzyme drag/prefactor fits. It makes crisp, falsifiable predictions: (i) cross-enzyme force-velocity collapse in reduced units, (ii) 1/T scaling of A and C at fixed ionic strength, and (iii) a pump-probe sideband at 3Ecoh.</p> |
| title | Parameter-Free DNA Mechanics and Transcription Kinetics from a Single 0.090 eV Quantum |
| url | https://doi.org/10.5281/zenodo.17102271 |