ChemRxiv
These are preliminary reports that have not been peer-reviewed. They should not be regarded as conclusive, guide clinical practice/health-related behavior, or be reported in news media as established information. For more information, please see our FAQs.
1/1
2 files
0/0

Energetic Self-Folding Mechanism in α-Helixes

preprint
submitted on 19.06.2019 and posted on 20.06.2019 by Adolfo Bastida, José Zúñiga, Alberto Requena, Javier Cerezo
A novel energetic route driving the folding of a polyalanine peptide from an extended conformation to its α-helix native conformation is described, supported by a new method to compute mean potential energy surfaces accurately in terms of the dihedral angles of the peptide chain from extensive Molecular Dynamics simulations. The Energetic Self-Folding (ESF) route arises specifically from the balance between the intrinsic propensity of alanine residues towards the αR conformation and two, opposite, effects: the destabilizing interaction with neighbor residues and the stabilizing formation of native hydrogen bonds, with the latter being dominant for large peptide lengths. The ESF mechanism provides simple but robust support to the nucleation-elongation, or zipper models, and offers a quantitative energetic funnel picture of the folding process. The mechanism is validated by the reasonable agreement between the computed folding energies and the experimental values.

History

Email Address of Submitting Author

bastida@um.es

Institution

Universidad de Murcia

Country

Spain

ORCID For Submitting Author

0000-0002-8193-9233

Declaration of Conflict of Interest

The authors declare no competing financial interests.

Exports

Logo branding

Exports