Allostery as Electromagnetic Field Propagation Through Protein Geometry

Abstract Allostery—the transmission of regulatory signals across protein structures—is one of molecular biology’s most fundamental yet mechanistically elusive phenomena. Structural and dynamic studies document global conformational coupling between distant protein domains with no identifiable physical pathway connecting them. Consensus frameworks describe the observations (entropy redistribution, ensemble shifts, dynamic networks) but provide no mechanistic explanation for how binding at one site affects distant sites. We present an explicit mechanism: proteins are continuous electromagnetic field structures—origami of polarity expression—where ligand binding creates local geometric constraint that propagates sequentially through the structure as a cascade of shifting polarities, driving the system toward a new stable configuration. This is not diffusive signaling through specific amino acid pathways—it is electromagnetic field propagation through continuous protein geometry. Using kinesin motor protein as detailed example, we show how ATP binding initiates a deterministic geometric cascade: polarity recognition → Mode B lock → local disparity → sequential propagation → ATP integration with byproduct ejection → protein reset for next cycle. Electromagnetic gradients drive motion. Motion generates heat. Heat increases activity. No vitalism. No energy currency. Pure geometric determinism. Cellular specificity emerges not from statistical luck in “crowded zoos” of randomly colliding particles, but from geometric recognition—molecules attracted to complementary polarities, repelled from incompatible ones. “Right” collisions are geometric inevitability, not statistical miracle. This mechanism provides three testable investigations derived directly from core principles: one exploratory probe mapping geometric cascade sensitivity, two critical tests with clear discriminating outcomes. All falsifiable with existing experimental techniques and all await testing. The mechanism derives from scale-invariant principles: gradients (electromagnetic, thermal, concentration) + geometry → cascades → stable states. The gradient type varies by scale and system; the principle does not. Life is geometry. Proteins are the origami of electromagnetic/polarity expression. Biology is geometry dancing. Keywords: allostery, protein dynamics, ATP mechanism, motor proteins, enzyme catalysis, electromagnetic cascade, geometric constraints, neuroplasticity, prion propagation, scale invariance