Publication:
Proteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures

dc.contributor.authorBianco, Valentino
dc.contributor.authorAlonso-Navarro, Miren
dc.contributor.authorDi Silvio, Desire
dc.contributor.authorMoya, Sergio
dc.contributor.authorCortajarena L., Aitziber
dc.contributor.authorColuzza, Ivan
dc.date.accessioned2023-06-17T13:28:08Z
dc.date.available2023-06-17T13:28:08Z
dc.date.issued2019
dc.description.abstractWe present a computational and experimental study on the folding and aggregation in solutions of multiple protein mixtures at different concentrations. We show how in protein mixtures, each component is capable of maintaining its folded state at desensitises higher then the one at which they would precipitate in single species solutions. We demonstrate the generality of our observation over many different proteins using computer simulations capable of fully characterising the cross-aggregation phase diagram of all the mixtures. Dynamic light Scattering experiments were performed to evaluate the aggregation of two proteins, the bovine serum albumin (BSA) and the consensus tetratricopeptide repeat (CTPR), in solutions of one or both proteins. The experiment confirm our hypothesis and the simulations. These findings elucidate critical aspects on the cross-regulation of expression and aggregation of proteins exerted by the cell and on the evolutionary selection of folding and not-aggregating protein sequences, paving the way for new experimental tests.
dc.description.departmentDepto. de Química Física
dc.description.facultyFac. de Ciencias Químicas
dc.description.refereedTRUE
dc.description.sponsorshipUnión Europea. H2020
dc.description.sponsorshipMinisterio de Economía y Competitividad (MINECO)
dc.description.sponsorshipAustrian Science Fund (FWF)
dc.description.sponsorshipUnidad de Excelencia "María de Maeztu"
dc.description.sponsorshipBasque Government
dc.description.statusinpress
dc.eprint.idhttps://eprints.ucm.es/id/eprint/57003
dc.identifier.issn1948-7185
dc.identifier.officialurlhttps://doi.org/10.1021/acs.jpclett.9b01753
dc.identifier.relatedurlhttps://doi.org/10.1021/acs.jpclett.9b01753
dc.identifier.urihttps://hdl.handle.net/20.500.14352/13559
dc.issue.number17
dc.journal.titleThe Journal of Physical Chemistry Letters
dc.language.isoeng
dc.page.final4807
dc.page.initial4800
dc.publisherACS
dc.relation.projectIDProFrost (748170)
dc.relation.projectID(BIO2016-77367-C2-1-R); (FIS2017-89471-R)
dc.relation.projectIDM 2150-N36
dc.relation.projectIDMDM-2017-0720
dc.relation.projectIDElkartek KK-2017/00008
dc.relation.projectIDP 26253-N27
dc.rights.accessRightsopen access
dc.subject.cdu544
dc.subject.keywordLight scattering
dc.subject.keywordMammals
dc.subject.keywordMixtures
dc.subject.ucmFísica (Física)
dc.subject.ucmTermodinámica
dc.subject.ucmQuímica
dc.subject.ucmBiología
dc.subject.unesco22 Física
dc.subject.unesco2213 Termodinámica
dc.subject.unesco23 Química
dc.subject.unesco24 Ciencias de la Vida
dc.titleProteins Are Solitary! Pathways of Protein Folding and Aggregation in Protein Mixtures
dc.typejournal article
dc.volume.number10
dspace.entity.typePublication
relation.isAuthorOfPublicationbab899d3-b920-429c-9061-5d0cefd5d756
relation.isAuthorOfPublication.latestForDiscoverybab899d3-b920-429c-9061-5d0cefd5d756
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