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dc.contributor.authorMoreno Segurado, Ángel J.-
dc.contributor.authorLo Verso, Federica-
dc.contributor.authorArbe, Arantxa-
dc.contributor.authorPomposo, José A.-
dc.contributor.authorColmenero de León, Juan-
dc.date.accessioned2016-09-23T09:10:14Z-
dc.date.available2016-09-23T09:10:14Z-
dc.date.issued2016-
dc.identifierdoi: 10.1021/acs.jpclett.6b00144-
dc.identifiere-issn: 1948-7185-
dc.identifier.citationJournal of Physical Chemistry Letters 7(5): 838-844 (2016)-
dc.identifier.urihttp://hdl.handle.net/10261/137266-
dc.description.abstractBy means of large-scale computer simulations and small-angle neutron scattering (SANS), we investigate solutions of single-chain nanoparticles (SCNPs), covering the whole concentration range from infinite dilution to melt density. The analysis of the conformational properties of the SCNPs reveals that these synthetic nano-objects share basic ingredients with intrinsically disordered proteins (IDPs), as topological polydispersity, generally sparse conformations, and locally compact domains. We investigate the role of the architecture of the SCNPs in their collapse behavior under macromolecular crowding. Unlike in the case of linear macromolecules, which experience the usual transition from self-avoiding to Gaussian random-walk conformations, crowding leads to collapsed conformations of SCNPs resembling those of crumpled globules. This behavior is already found at volume fractions (about 30%) that are characteristic of crowding in cellular environments. The simulation results are confirmed by the SANS experiments. Our results for SCNPs - a model system free of specific interactions - propose a general scenario for the effect of steric crowding on IDPs: collapse from sparse conformations at high dilution to crumpled globular conformations in cell environments.-
dc.description.sponsorshipFinancial support from the Projects MAT2012-31088 and IT-654-13 (GV) is acknowledged. This work is based on experiments performed at SANS-1 (SINQ, Paul Scherrer Institute, Villigen, Switzerland), and KWS-2 (Heinz Maier-Leibnitz Zentrum (MLZ), Garching, Germany), and has been supported by the European Commission under the seventh Framework Programme through the ‘Research Infrastructures’ action of the ‘Capacities’ Programme, NMI3-II Grant Number 283883.-
dc.publisherAmerican Chemical Society-
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/283883-
dc.relation.isversionofPostprint-
dc.rightsopenAccessen_EN
dc.titleConcentrated solutions of single-chain nanoparticles: A simple model for intrinsically disordered proteins under crowding conditions-
dc.typeartículo-
dc.identifier.doihttp://dx.doi.org/10.1021/acs.jpclett.6b00144-
dc.relation.publisherversionhttp://dx.doi.org/10.1021/acs.jpclett.6b00144-
dc.date.updated2016-09-23T09:10:15Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderEusko Jaurlaritza-
dc.contributor.funderEuropean Commission-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003086es_ES
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