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dc.contributor.authorRomero Romero, María Luisa
dc.contributor.authorInglés Prieto, Álvaro
dc.contributor.authorIbarra Molero, Beatriz 
dc.contributor.authorSánchez Ruiz, José Manuel
dc.identifier.citationRomero Romero, M.L.; Inglés Prieto, A.; Ibarra Molero, B.; Sánchez Ruiz, J.M. Highly Anomalous Energetics of Protein Cold Denaturation Linked to Folding-Unfolding Kinetics. Plos One, 6(7): e23050 (2011). []es_ES
dc.identifier.otherdoi: 10.1371/journal.pone.0023050
dc.description.abstractDespite several careful experimental analyses, it is not yet clear whether protein cold-denaturation is just a “mirror image” of heat denaturation or whether it shows unique structural and energetic features. Here we report that, for a well-characterized small protein, heat denaturation and cold denaturation show dramatically different experimental energetic patterns. Specifically, while heat denaturation is endothermic, the cold transition (studied in the folding direction) occurs with negligible heat effect, in a manner seemingly akin to a gradual, second-order-like transition. We show that this highly anomalous energetics is actually an apparent effect associated to a large folding/unfolding free energy barrier and that it ultimately reflects kinetic stability, a naturally-selected trait in many protein systems. Kinetics thus emerges as an important factor linked to differential features of cold denaturation. We speculate that kinetic stabilization against cold denaturation may play a role in cold adaptation of psychrophilic organisms. Furthermore, we suggest that folding-unfolding kinetics should be taken into account when analyzing in vitro cold-denaturation experiments, in particular those carried out in the absence of destabilizing conditions.es_ES
dc.description.sponsorshipThis work was supported by FEDER (“Fondo Europeo de DEsarrollo Regional”) funds and Grants BIO2009-09562 and CSD2009-00088 from the Spanish Ministry of Science and Innovation.es_ES
dc.publisherPublic Library of Science (PLOS)es_ES
dc.rightsCreative Commons Attribution-NonCommercial-NoDerivs 3.0 Licensees_ES
dc.subjectCalorimetry es_ES
dc.subjectCircular dichroism spectroscopyes_ES
dc.subjectEnergetic materialses_ES
dc.subjectFree energyes_ES
dc.subjectRelaxation (physics)es_ES
dc.titleHighly Anomalous Energetics of Protein Cold Denaturation Linked to Folding-Unfolding Kineticses_ES

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