Structural characterization of the major ampullate silk spidroin-2 protein produced by the spider Nephila clavipes
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Data
2016-10-01
Autores
Aparecido dos Santos-Pinto, Jose Roberto [UNESP]
Arcuri, Helen Andrade [UNESP]
Lubec, Gert
Palma, Mario Sergio [UNESP]
Título da Revista
ISSN da Revista
Título de Volume
Editor
Elsevier B.V.
Resumo
Major ampullate spidroin-2 (MaSp2) is one of the most important spider silk protein, but up to now no information is available regarding the post-translational modifications (PTMs) of this protein. A gel-based mass spectrometry strategy using collision-induced dissociation (CID) and electron-transfer dissociation (ETD) fragmentation methods was used to sequence Nephila clavipes MaSp2 (including the N- and C-terminal non repetitive domains, and the great part of the central core), and to assign a series of post-translational modifications (PTMs) on to the MaSp2 sequence. Two forms of this protein were identified, with different levels of phosphorylation along their sequences. These findings provide a basis for understanding mechanoelastic properties and can support the future design of recombinant spider silk proteins for biotechnological applications. (C) 2016 Elsevier B.V. All rights reserved.
Descrição
Palavras-chave
Silk proteins, Nephila clavipes, Mass spectrometry, Post-translational modification, Phosphorylation
Como citar
Biochimica Et Biophysica Acta-proteins And Proteomics. Amsterdam: Elsevier Science Bv, v. 1864, n. 10, p. 1444-1454, 2016.