Show simple item record

dc.contributor.authorBastida Pascual, Adolfo 
dc.contributor.authorZúñiga Román, José 
dc.contributor.authorRequena Rodríguez, Alberto 
dc.contributor.authorMiguel Hernández, Beatriz 
dc.contributor.authorCerezo Bastida, Javier 
dc.date.accessioned2021-06-15T06:46:41Z
dc.date.available2021-06-15T06:46:41Z
dc.date.issued2020
dc.identifier.citationBastida A., Zúñiga J., Requena A., Miguel B., Cerezo J. On the Role of Entropy in the Stabilization of α-Helices. Journal of Chemical Information and Modeling. 2020 Dec;60(12):6523-6531. DOI: 10.1021/acs.jcim.0c01177.es_ES
dc.identifier.issn1549-960X
dc.description.abstractProtein 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 residueses_ES
dc.description.sponsorshipThis work was partially supported by the Spanish Agencia Estatal de Investigación (AEI) and Fondo Europeo de Desarrollo Regional (FEDER, UE) under Project CTQ2016-79345-P and by the Fundación Séeneca under Project 20789/PI/18. We thank the computational assistance provided by J. F. Hidalgo of the Servicio de Infraestructuras TIC de ATICA.es_ES
dc.formatapplication/pdfes_ES
dc.language.isoenges_ES
dc.publisherAmerican Chemical Societyes_ES
dc.rightsAtribución-NoComercial-SinDerivadas 3.0 España*
dc.rightsCopyright © 2020 ACSes_ES
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/es/*
dc.titleOn the role of entropy in the stabilization of α-Helixeses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.subjectEntropyes_ES
dc.subjectFree energyes_ES
dc.subjectPeptides and proteinses_ES
dc.subjectMoleculeses_ES
dc.subjectConformationes_ES
dc.subject.otherIngeniería Químicaes_ES
dc.identifier.urihttp://hdl.handle.net/10317/9434
dc.identifier.doi10.1021/acs.jcim.0c01177
dc.identifier.urlhttps://pubs.acs.org/doi/10.1021/acs.jcim.0c01177
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES
dc.type.versioninfo:eu-repo/semantics/submittedVersiones_ES
dc.relation.projectIDCTQ2016-79345-Pes_ES
dc.relation.projectID20789/PI/18es_ES
dc.subject.unesco2302.26 Bioquímica Físicaes_ES
dc.contributor.funderAgencia Estatal de Investigación (AEI)es_ES
dc.contributor.funderFondo Europeo de Desarrollo Regional (FEDER)es_ES


Files in this item

untranslated

This item appears in the following Collection(s)

Show simple item record

Atribución-NoComercial-SinDerivadas 3.0 España
Except where otherwise noted, this item's license is described as Atribución-NoComercial-SinDerivadas 3.0 España