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| Main Author: | |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Chirality
2026
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/42204377/ |
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Table of Contents:
- Geometric Stabilization of Biomolecular Chirality in Open Systems. Domínguez-Arca, Vicente Stereoisomerism Thermodynamics Models, Molecular Amino Acids Proteins Entropy The homochirality of life-the exclusive use of L-amino acids and the universal right-handedness of -helices-stands as one of the most persistent asymmetries in biology. While often attributed to kinetic or energetic biases, the overwhelming statistical dominance of these chiral forms still lacks a fully compelling thermodynamic and geometric explanation. Here, we propose a geometric mechanism for the stabilization and amplification of biomolecular handedness in open, entropy-producing systems. By introducing a local chirality marker based on the sign of a scalar triple product (equivalently, the sign of a determinant built from atomic coordinate differences and the local helical axis), we show that right-handed -helices can be can be represented as orientation-preserving sectors of the local configuration space in the local configuration space. Under physically admissible continuous backbone moves, chirality inversion requires crossing a degenerate subset where the marker vanishes, which constitutes a lower dimensional region of effectively zero measure in the feasible configuration manifold. Consequently, parity-inverting pathways are dynamically suppressed, and once a chiral sign becomes established, it tends to persist and amplify under irreversible evolution consistent with least-time free-energy dissipation. Our framework reframes biomolecular homochirality not as the consequence of a primordial energetic asymmetry but as an emergent, statistically stabilized standard arising from the interplay between nonequilibrium thermodynamics and the geometry of configuration space.