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Fast NMR method to probe solvent accessibility and disordered regions in proteins

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dc.contributor.authorFaustino, André F.
dc.contributor.authorBarbosa, Glauce M.
dc.contributor.authorSilva, Micael
dc.contributor.authorCastanho, Miguel
dc.contributor.authorDa Poian, Andrea T .
dc.contributor.authorCabrita, Eurico J.
dc.contributor.authorSantos, Nuno C.
dc.contributor.authorAlmeida, Fabio C. L.
dc.contributor.authorMartins, Ivo C.
dc.date.accessioned2019-04-12T15:31:26Z
dc.date.available2019-04-12T15:31:26Z
dc.date.issued2019
dc.description© Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. Te images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.pt_PT
dc.description.abstractUnderstanding protein structure and dynamics, which govern key cellular processes, is crucial for basic and applied research. Intrinsically disordered protein (IDP) regions display multifunctionality via alternative transient conformations, being key players in disease mechanisms. IDP regions are abundant, namely in small viruses, allowing a large number of functions out of a small proteome. The relation between protein function and structure is thus now seen from a different perspective: as IDP regions enable transient structural arrangements, each conformer can play different roles within the cell. However, as IDP regions are hard and time-consuming to study via classical techniques (optimized for globular proteins with unique conformations), new methods are required. Here, employing the dengue virus (DENV) capsid (C) protein and the immunoglobulin-binding domain of streptococcal protein G, we describe a straightforward NMR method to differentiate the solvent accessibility of single amino acid N-H groups in structured and IDP regions. We also gain insights into DENV C flexible fold region biological activity. The method, based on minimal pH changes, uses the well-established 1H-15N HSQC pulse sequence and is easily implementable in current protein NMR routines. The data generated are simple to interpret, with this rapid approach being an useful first-choice IDPs characterization method.pt_PT
dc.description.sponsorshipThis work was supported by Fundação para a Ciência e a Tecnologia – Ministério da Ciência, Tecnologia e Ensino Superior (FCT-MCTES, Portugal) projects PTDC/QUI-BIQ/112929/2009, PTDC/SAU-ENB/117013/2010 and PTDC/BBB-BQB/3494/2014, Calouste Gulbenkian Foundation (FCG, Portugal) project Science Frontiers Research Prize 2010, European Union Marie Skłodowska-Curie Research and Innovation Staff Exchange H2020-MSCA-RISE-2014 project INPACT (Grant 644167), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq, Brazil, grant numbers 471239/2012-7 and 306669/2013-7) and Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ, Brazil, grant numbers E-26/110.636/2012, E-26/110.092/2013 and E-26/201.167/2014). AFF acknowledges FCT-MCTES fellowship SFRH/BD/77609/2011. MS acknowledges FCT-MCTES fellowship PD/BD/128202/2016. ICM acknowledges consecutive funding from the FCT-MCTES fellowship SFRH/BPD/74287/2010 and the Program “Investigador FCT” (IF/00772/2013 Research Contract). This work was also supported by LISBOA01-0145-FEDER-007391 project, cofounded by FEDER, through POR Lisboa 2020 - Programa Operacional Regional de Lisboa, PORTUGAL 2020, and Fundação para a Ciência e a Tecnologia. The NMR spectrometers at FCT NOVA are part of Rede Nacional de RMN (PTNMR), supported by FCT-MCTES (ROTEIRO/0031/2013 - PINFRA/22161/2016) co-funded by FEDER through COMPETE 2020, POCI, and PORL and FCT through PIDDAC.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationScientific Reports (2019) 9:1647pt_PT
dc.identifier.doi10.1038/s41598-018-37599-zpt_PT
dc.identifier.issn2045-2322
dc.identifier.urihttp://hdl.handle.net/10451/37911
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherNature Researchpt_PT
dc.relation644167pt_PT
dc.relationBroad-spectrum antiviral peptides against respiratory viruses
dc.relationIF/00772/2013pt_PT
dc.relationDENGUE VIRUS REPLICATION: THE INTERPLAY BETWEEN LIPID DROPLETS AND THE CAPSID PROTEIN
dc.relationNMR investigation of ion-pair modulation of protein structure and dynamics and its relation to protein misfolding diseases
dc.relationPortuguese Nuclear Magnetic Resonance Network
dc.relation.publisherversionhttps://www.nature.com/srep/pt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleFast NMR method to probe solvent accessibility and disordered regions in proteinspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleBroad-spectrum antiviral peptides against respiratory viruses
oaire.awardTitleDENGUE VIRUS REPLICATION: THE INTERPLAY BETWEEN LIPID DROPLETS AND THE CAPSID PROTEIN
oaire.awardTitleNMR investigation of ion-pair modulation of protein structure and dynamics and its relation to protein misfolding diseases
oaire.awardTitlePortuguese Nuclear Magnetic Resonance Network
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F112929%2F2009/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FSAU-ENB%2F117013%2F2010/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FBBB-BQB%2F3494%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F77609%2F2011/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//PD%2FBD%2F128202%2F2016/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F74287%2F2010/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/9444 - RNIIIE/PINFRA%2F22161%2F2016/PT
oaire.citation.issue1pt_PT
oaire.citation.startPage1647pt_PT
oaire.citation.titleScientific Reportspt_PT
oaire.citation.volume9pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStreamSFRH
oaire.fundingStream9444 - RNIIIE
person.familyNameda Costa Faustino
person.familyNameCastanho
person.familyNameSantos
person.familyNameMartins
person.givenNameAndré Filipe
person.givenNameMiguel
person.givenNameNuno
person.givenNameIvo
person.identifier.ciencia-id3D19-A07A-6E7C
person.identifier.ciencia-idCD13-5E3A-A3C5
person.identifier.ciencia-id8C17-BB8B-E8DB
person.identifier.orcid0000-0002-7364-8524
person.identifier.orcid0000-0001-7891-7562
person.identifier.orcid0000-0002-0580-0475
person.identifier.orcid0000-0002-9284-8599
person.identifier.ridN-7248-2013
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person.identifier.scopus-author-id56605575600
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project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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