Dominant folding pathways of a peptide chain, from ab-initio quantum-mechanical simulations

2010/07/29 by S. a Beccara, Beccara, S. a, Pietro Faccioli +14
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Advanced Chemical Physics Studies #Biomolecules (q-bio.BM) #FOS: Biological sciences #FOS: Physical sciences #Protein Structure and Dynamics #Soft Condensed Matter (cond-mat.soft) #Spectroscopy and Quantum Chemical Studies #Strongly Correlated Electrons (cond-mat.str-el) #cond-mat.soft #cond-mat.str-el #q-bio.BM

paper · pdf · doi:10.48550/arxiv.1007.5235

9 pages, 5 figures

arxiv created 2010/07/29 · openalex publication_date 2010/07/29 · arxiv updated 2010/07/30 · openalex created_date 2019/06/27 · openalex updated_date 2026/07/28

Abstract

Using the Dominant Reaction Pathways method, we perform an ab-initio quantum-mechanical simulation of a conformational transition of a peptide chain. The method we propose makes it possible to investigate the out-of-equilibrium dynamics of these systems, without resorting to an empirical representation of the molecular force field. It also allows to study rare transitions involving rearrangements in the electronic structure. By comparing the results of the ab-initio simulation with those obtained employing a standard force field, we discuss its capability to describe the non-equilibrium dynamics of conformational transitions.

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