Structural Model for the Spider Silk Protein Spidroin-1

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dc.contributor.authorAparecido dos Santos-Pinto, Jose Roberto [UNESP]
dc.contributor.authorArcuri, Helen Andrade [UNESP]
dc.contributor.authorPriewalder, Helga
dc.contributor.authorSalles, Heliana Clara [UNESP]
dc.contributor.authorPalma, Mario Sergio [UNESP]
dc.contributor.authorLubec, Gert
dc.contributor.institutionUniversidade Estadual Paulista (Unesp)
dc.contributor.institutionMed Univ Vienna
dc.contributor.institutionGeol Survey Austria
dc.date.accessioned2018-11-26T16:16:47Z
dc.date.available2018-11-26T16:16:47Z
dc.date.issued2015-09-01
dc.description.abstractMost reports about the 3-D structure of spidroin-1 have been proposed for the protein in solid state or for individual domains of these proteins. A gel-based mass spectrometry strategy using collision-induced dissociation (CID) and electron-transfer dissociation (ETD) fragmentation methods was used to completely sequence spidroins-1A and -1B and to assign a series of post-translational modifications (PTMs) on to the spidroin sequences. A total of 15 and 16 phosphorylation sites were detected on spidroin-1A and -1B, respectively. In this work, we present the nearly complete amino acid sequence of spidroin-1A and -1B, including the nonrepetitive N- and C-terminal domains and a highly repetitive central core. We also described a fatty acid layer surrounding the protein fibers and PTMs in the sequences of spidroin-1A and -1B, including phosphorylation. Thus, molecular models for phosphorylated spidroins were proposed in the presence of a mixture fatty acids/water (1:1) and submitted to molecular dynamics simulation. The resulting models presented high content of coils, a higher percentage of alpha-helix, and an almost neglected content of 3(10)-helix than the previous models. Knowledge of the complete structure of spidroins-1A and -1B would help to explain the mechanical features of silk fibers. The results of the current investigation provide a foundation for biophysical studies of the mechanoelastic properties of web-silk proteins.en
dc.description.affiliationSao Paulo State Univ, Ctr Study Social Insects, Inst Biosci Rio Claro, Dept Biol, BR-13500 Rio Claro, SP, Brazil
dc.description.affiliationMed Univ Vienna, Dept Pediat, A-1090 Vienna, Austria
dc.description.affiliationGeol Survey Austria, Dept Paleontol, A-1230 Vienna, Austria
dc.description.affiliationUnespSao Paulo State Univ, Ctr Study Social Insects, Inst Biosci Rio Claro, Dept Biol, BR-13500 Rio Claro, SP, Brazil
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipGert Lubec Proteomics Laboratory at the University of Vienna
dc.description.sponsorshipIdFAPESP: 2010/19051-6
dc.description.sponsorshipIdFAPESP: 2011/51684-1
dc.description.sponsorshipIdFAPESP: 2013/26451-9
dc.description.sponsorshipIdCNPq: 301656/2013-4
dc.format.extent3859-3870
dc.identifierhttp://dx.doi.org/10.1021/acs.jproteome.5b00243
dc.identifier.citationJournal Of Proteome Research. Washington: Amer Chemical Soc, v. 14, n. 9, p. 3859-3870, 2015.
dc.identifier.doi10.1021/acs.jproteome.5b00243
dc.identifier.issn1535-3893
dc.identifier.lattes2901888624506535
dc.identifier.urihttp://hdl.handle.net/11449/160797
dc.identifier.wosWOS:000361087100039
dc.language.isoeng
dc.publisherAmer Chemical Soc
dc.relation.ispartofJournal Of Proteome Research
dc.relation.ispartofsjr1,818
dc.rights.accessRightsAcesso restrito
dc.sourceWeb of Science
dc.subjectsilk proteins
dc.subjectNephila clavipes
dc.subjectmass spectrometry
dc.subjectpost-translational modification
dc.subjectmolecular dynamics
dc.titleStructural Model for the Spider Silk Protein Spidroin-1en
dc.typeArtigo
dcterms.rightsHolderAmer Chemical Soc
unesp.author.lattes2901888624506535
unesp.author.orcid0000-0002-6333-9461[6]

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