Spider silk proteome provides insight into the structural characterization of Nephila clavipes flagelliform spidroin

Registro completo de metadados
MetadadosDescriçãoIdioma
Autor(es): dc.contributorUniversidade Estadual Paulista (UNESP)-
Autor(es): dc.creatorAparecido dos Santos-Pinto, Jose Roberto-
Autor(es): dc.creatorArcuri, Helen Andrade-
Autor(es): dc.creatorEsteves, Franciele Grego-
Autor(es): dc.creatorPalma, Mario Sergio-
Autor(es): dc.creatorLubec, Gert-
Data de aceite: dc.date.accessioned2021-03-11T01:13:24Z-
Data de disponibilização: dc.date.available2021-03-11T01:13:24Z-
Data de envio: dc.date.issued2019-10-04-
Data de envio: dc.date.issued2019-10-04-
Data de envio: dc.date.issued2018-10-02-
Fonte completa do material: dc.identifierhttp://dx.doi.org/10.1038/s41598-018-33068-9-
Fonte completa do material: dc.identifierhttp://hdl.handle.net/11449/184884-
Fonte: dc.identifier.urihttp://educapes.capes.gov.br/handle/11449/184884-
Descrição: dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)-
Descrição: dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)-
Descrição: dc.descriptionGert Lubec Proteomics Laboratory-
Descrição: dc.descriptionProcesso FAPESP: 2010/19051-6-
Descrição: dc.descriptionProcesso FAPESP: 2011/51684-1-
Descrição: dc.descriptionProcesso FAPESP: 2013/26451-9-
Descrição: dc.descriptionProcesso FAPESP: 2015/14220-8-
Descrição: dc.descriptionProcesso FAPESP: 2016/16212-5-
Descrição: dc.descriptionCNPq: 301656/2013-4-
Descrição: dc.descriptionCNPq: 150699/2017-4-
Descrição: dc.descriptionThe capture spiral of web from N. clavipes spider consists of a single type of spidroin - the flagelliform silk protein, a natural material representing a combination of strength and high elasticity. Flagelliform spider silk is the most extensible silk fibre produced by orb weaver spiders and the structure of this remarkable material is still largely unknown. In the present study we used a proteomic approach to elucidate the complete sequence and the post-translational modifications of flagelliform silk proteins. The long sequence of flagelliform silk protein presents 45 hydroxylated proline residues, which may contribute to explain the mechanoelastic property of these fibres, since they are located in the GPGGX motif. The 3D-structure of the protein was modelled considering the three domains together, i.e., the N- and C-terminal non-repetitive domains, and the central repetitive domain. In the resulting molecular model there is a predominance of random structures in the solid fibres of the silk protein. The N-terminal domain is composed of three alpha-helices and the C-terminal domain is composed of one small helical section. Proteomic data reported herein may be relevant for the development of novel approaches for the synthetic or recombinant production of novel silk-based spider polymers.-
Formato: dc.format12-
Idioma: dc.languageen-
Publicador: dc.publisherNature Publishing Group-
Relação: dc.relationScientific Reports-
Direitos: dc.rightsopenAccess-
Título: dc.titleSpider silk proteome provides insight into the structural characterization of Nephila clavipes flagelliform spidroin-
Tipo de arquivo: dc.typelivro digital-
Aparece nas coleções:Repositório Institucional - Unesp

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