Folding of a helix is critically stabilized by polarization of backbone hydrogen bonds: study in explicit water
| Autor: | John Z. H. Zhang, Bo Tang, Ya Gao, Ye Mei, Qing G. Zhang, Li L. Duan |
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| Rok vydání: | 2012 |
| Předmět: |
chemistry.chemical_classification
Protein Folding Chemistry Hydrogen bond Protein Data Bank (RCSB PDB) Beta sheet Temperature Water Peptide Hydrogen Bonding Molecular Dynamics Simulation Protein Structure Secondary Surfaces Coatings and Films Molecular dynamics Crystallography Materials Chemistry Cluster Analysis Physical and Theoretical Chemistry Peptides Protein secondary structure Alpha helix Polyproline helix |
| Zdroj: | The journal of physical chemistry. B. 116(10) |
| ISSN: | 1520-5207 |
| Popis: | Multiple single-trajectory molecular dynamics (MD) simulation at room temperature (300 K) in explicit water was carried out to study the folding dynamics of an α-helix (PDB 2I9M ) using a polarized charge scheme that includes electronic polarization of backbone hydrogen bonds. Starting from an extended conformation, the 17-residue peptide was successfully folded into the native structure (α-helix) between 80 and 130 ns with a root-mean-square deviation of ~1.0 Å. Analysis of the time-dependent trajectories revealed that helix formation of the peptide started at the terminals and progressed toward the center of the peptide. For comparison, MD trajectories generated under various versions of standard AMBER force fields failed to show any significant or stable helix formation in our simulation. Our result shows clear evidence that the electronic polarization of backbone hydrogen bonds energetically stabilizes the helix formation and is critical to the stable folding of the short helix structure. |
| Databáze: | OpenAIRE |
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