13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation

Detalhes bibliográficos
Autor(a) principal: Ribeiro,Tatiana Santana
Data de Publicação: 2022
Outros Autores: Scramin,Juliana Aparecida, Rodrigues,José Avelino Santos, Bernardes Filho,Rubens, Colnago,Luiz Alberto, Forato,Lucimara Aparecida
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Polímeros (São Carlos. Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282022000100407
Resumo: Abstract Kafirins, water-insoluble proteins from Sweet Sorghum BR501 grains, have been an alternative to prepare edible coatings for food due to their hydrophobic character. In this work, the secondary structures (SS) content of reduced (SSr) and unreduced (SSu) kafirins were determined by 13C solid-state-NMR spectroscopy using areas of carbonyl peak. The SS elucidate by fitting the signal with the Lorentzian function shows 56% and 59% of α-helix and 40% and 12% of β-sheet structures for SSr and SSu, respectively. The SS also were elucidated by a Singular value decomposition- SVD method shows 55% and 49% of α-helix and 12% and 8% of β-sheet structure for SSr and SSu, respectively. Since SVD does not depend on the operator and has higher correlation coefficients for α-helix (0.96%) and β-sheet (0.91%), it is a reliable method to quantify the SS of insoluble proteins using the 13C NMR signal.
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spelling 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidationkafirinsecondary structures proteinssweet sorghuminsoluble proteinsolid-state 13C NMR spectroscopyAbstract Kafirins, water-insoluble proteins from Sweet Sorghum BR501 grains, have been an alternative to prepare edible coatings for food due to their hydrophobic character. In this work, the secondary structures (SS) content of reduced (SSr) and unreduced (SSu) kafirins were determined by 13C solid-state-NMR spectroscopy using areas of carbonyl peak. The SS elucidate by fitting the signal with the Lorentzian function shows 56% and 59% of α-helix and 40% and 12% of β-sheet structures for SSr and SSu, respectively. The SS also were elucidated by a Singular value decomposition- SVD method shows 55% and 49% of α-helix and 12% and 8% of β-sheet structure for SSr and SSu, respectively. Since SVD does not depend on the operator and has higher correlation coefficients for α-helix (0.96%) and β-sheet (0.91%), it is a reliable method to quantify the SS of insoluble proteins using the 13C NMR signal.Associação Brasileira de Polímeros2022-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282022000100407Polímeros v.32 n.1 2022reponame:Polímeros (São Carlos. Online)instname:Associação Brasileira de Polímeros (ABPol)instacron:ABPO10.1590/0104-1428.20210082info:eu-repo/semantics/openAccessRibeiro,Tatiana SantanaScramin,Juliana AparecidaRodrigues,José Avelino SantosBernardes Filho,RubensColnago,Luiz AlbertoForato,Lucimara Aparecidaeng2022-05-02T00:00:00Zoai:scielo:S0104-14282022000100407Revistahttp://www.scielo.br/pohttps://old.scielo.br/oai/scielo-oai.php||revista@abpol.org.br1678-51690104-1428opendoar:2022-05-02T00:00Polímeros (São Carlos. Online) - Associação Brasileira de Polímeros (ABPol)false
dc.title.none.fl_str_mv 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
title 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
spellingShingle 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
Ribeiro,Tatiana Santana
kafirin
secondary structures proteins
sweet sorghum
insoluble protein
solid-state 13C NMR spectroscopy
title_short 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
title_full 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
title_fullStr 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
title_full_unstemmed 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
title_sort 13C ss-NMR Singular value decomposition and fitting for sorghum proteins conformation elucidation
author Ribeiro,Tatiana Santana
author_facet Ribeiro,Tatiana Santana
Scramin,Juliana Aparecida
Rodrigues,José Avelino Santos
Bernardes Filho,Rubens
Colnago,Luiz Alberto
Forato,Lucimara Aparecida
author_role author
author2 Scramin,Juliana Aparecida
Rodrigues,José Avelino Santos
Bernardes Filho,Rubens
Colnago,Luiz Alberto
Forato,Lucimara Aparecida
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Ribeiro,Tatiana Santana
Scramin,Juliana Aparecida
Rodrigues,José Avelino Santos
Bernardes Filho,Rubens
Colnago,Luiz Alberto
Forato,Lucimara Aparecida
dc.subject.por.fl_str_mv kafirin
secondary structures proteins
sweet sorghum
insoluble protein
solid-state 13C NMR spectroscopy
topic kafirin
secondary structures proteins
sweet sorghum
insoluble protein
solid-state 13C NMR spectroscopy
description Abstract Kafirins, water-insoluble proteins from Sweet Sorghum BR501 grains, have been an alternative to prepare edible coatings for food due to their hydrophobic character. In this work, the secondary structures (SS) content of reduced (SSr) and unreduced (SSu) kafirins were determined by 13C solid-state-NMR spectroscopy using areas of carbonyl peak. The SS elucidate by fitting the signal with the Lorentzian function shows 56% and 59% of α-helix and 40% and 12% of β-sheet structures for SSr and SSu, respectively. The SS also were elucidated by a Singular value decomposition- SVD method shows 55% and 49% of α-helix and 12% and 8% of β-sheet structure for SSr and SSu, respectively. Since SVD does not depend on the operator and has higher correlation coefficients for α-helix (0.96%) and β-sheet (0.91%), it is a reliable method to quantify the SS of insoluble proteins using the 13C NMR signal.
publishDate 2022
dc.date.none.fl_str_mv 2022-01-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282022000100407
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0104-14282022000100407
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/0104-1428.20210082
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Associação Brasileira de Polímeros
publisher.none.fl_str_mv Associação Brasileira de Polímeros
dc.source.none.fl_str_mv Polímeros v.32 n.1 2022
reponame:Polímeros (São Carlos. Online)
instname:Associação Brasileira de Polímeros (ABPol)
instacron:ABPO
instname_str Associação Brasileira de Polímeros (ABPol)
instacron_str ABPO
institution ABPO
reponame_str Polímeros (São Carlos. Online)
collection Polímeros (São Carlos. Online)
repository.name.fl_str_mv Polímeros (São Carlos. Online) - Associação Brasileira de Polímeros (ABPol)
repository.mail.fl_str_mv ||revista@abpol.org.br
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