The parity-violation energy difference between enantiomeric forms of the same amino acid sequence, from the amyloid beta-peptide involved in Alzheimer's desease, in both alpha-helix and beta-sheet configurations, is investigated with ab-initio techniques. To this end, we develop an extension of the N2 computational scheme that selectively includes neighboring amino acids to preserve the relevant H-bonds. In agreement with previous speculations, it is found that the helical alpha structure is associated with larger parity-violation energy differences than the corresponding beta form. Implications for the evolution of biological homochirality are discussed as well as the relative importance of various effects in determining the parity-violation energy.
Parity-Violation Energy of Biomolecules-IV: Protein Secondary Structure / Faglioni, Francesco; I., Garcia Cuesta. - In: ORIGINS OF LIFE AND EVOLUTION OF THE BIOSPHERE. - ISSN 0169-6149. - STAMPA. - 41:3(2011), pp. 249-259. [10.1007/s11084-010-9229-7]
Parity-Violation Energy of Biomolecules-IV: Protein Secondary Structure
FAGLIONI, Francesco;
2011
Abstract
The parity-violation energy difference between enantiomeric forms of the same amino acid sequence, from the amyloid beta-peptide involved in Alzheimer's desease, in both alpha-helix and beta-sheet configurations, is investigated with ab-initio techniques. To this end, we develop an extension of the N2 computational scheme that selectively includes neighboring amino acids to preserve the relevant H-bonds. In agreement with previous speculations, it is found that the helical alpha structure is associated with larger parity-violation energy differences than the corresponding beta form. Implications for the evolution of biological homochirality are discussed as well as the relative importance of various effects in determining the parity-violation energy.File | Dimensione | Formato | |
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