Identifies a new mechanism for protein folding in biophysics, suggesting improved understanding of molecular interactions.
DESCRIPTION:This work completes the protein folding problem by supplying the mechanism biophysics lacks. Proteins fold rapidly and reliably despite an astronomically large configuration space. Existing theories describe partial mechanisms but do not explain how proteins converge on the correct structure so quickly. Using the Carlo Framework, this paper introduces the contradiction engine, the trajectory update rule, and the Reset Operator > as the missing structural components that mechanise folding. The completed model treats the conflict between local interactions and global structural requirements as a contradiction loop. When this loop exceeds tolerance, the Carlo reset mechanism produces the native conformation. This paper formalises the folding contradiction, defines the reset threshold, and provides a unified mechanism linking chemical interactions to rapid structural convergence. KEYWORDS:protein folding, Levinthal’s paradox, folding pathways, native conformation, hydrophobic collapse, secondary structure, tertiary structure, folding funnel, energy landscape, misfolding, chaperones, molecular biology, biophysics, contradiction engine, Carlo Framework, Reset Operator, trajectory update rule, folding dynamics, structural specificity, foundational biology, theoretical biology, dynamic systems, system reorganisation, contradiction loops, threshold dynamics, structural completion, mechanism-level explanation, folding kinetics, conformational search, molecular interactions, folding stability, misfold correction, protein structure formation, emergent structure, folding operators, dynamic resolution, folding architecture, molecular contradictions, system evolution, biological structure, folding modelling, structural emergence, folding thresholds, protein behaviour, folding mechanism
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Carlo et al. (2026) studied this question.
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