On the role of entropy in the stabilization of α-helices
Entity
UAM. Departamento de QuímicaPublisher
ACS PublicationsDate
2020-12-28Citation
10.1021/acs.jcim.0c01177
Journal of Chemical Information and Modeling 60.12 (2020): 6523-6531
ISSN
1549-9596DOI
10.1021/acs.jcim.0c01177Funded by
This work was partially supported by the Spanish AgenciaEstatal de Investigación (AEI) and Fondo Europeo de Desarrollo Regional (FEDER, UE) under Project CTQ2016-79345-P and by the Fundación Séneca under Project 20789/PI/18. We thank the computational assistance provided by J.F.Hidalgo of the Servicio de Infraestructuras TIC de ATICAProject
Gobierno de España. CTQ2016-79345-PEditor's Version
https://doi.org/10.1021/acs.jcim.0c01177Subjects
QuímicaRights
© 2020 American Chemical SocietyEsta obra está bajo una licencia de Creative Commons Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional.
Abstract
Protein folding evolves by exploring the conformational space with a subtle balance between enthalpy and entropy changes which eventually leads to a decrease of free energy upon reaching the folded structure. A complete understanding of this process requires, therefore, a deep insight into both contributions to free energy. In this work, we clarify the role of entropy in favoring the stabilization of folded structures in polyalanine peptides with up to 12 residues. We use a novel method referred to as K2V that allows us to obtain the potential-energy landscapes in terms of residue conformations extracted from molecular dynamics simulations at conformational equilibrium and yields folding thermodynamic magnitudes, which are in agreement with the experimental data available. Our results demonstrate that the folded structures of the larger polyalanine chains are stabilized with respect to the folded structures of the shorter chains by both an energetic contribution coming from the formation of the intramolecular hydrogen bonds and an entropic contribution coming from an increase of the entropy of the solvent with approximate weights of 60 and 40%, respectively, thus unveiling a key piece in the puzzle of protein folding. In addition, the ability of the K2V method to provide the enthalpic and entropic contributions for individual residues along the peptide chain makes it clear that the energetic and entropic stabilizations are basically governed by the nearest neighbor residue conformations, with the folding propensity being rationalized in terms of triads of residues
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Google Scholar:Bastida, Adolfo
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Zúñiga, José
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Requena, Alberto
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Miguel, Beatriz
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Cerezo, Javier
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Zúñiga, Jose
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Requena, Alberto
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Miguel, Beatriz
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Cerezo Bastida, Javier
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