Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics
Autor(a) principal: | |
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Data de Publicação: | 2006 |
Outros Autores: | , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Genetics and Molecular Biology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030 |
Resumo: | With the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13C, 15N and ¹H chemical shift dispersion to predict the amount of secondary structure of unassigned proteins from their 15N- and/or 13C-edited heteronuclear single quantum coherence (HSQC) spectra. This methodology has been coded into a software called PASSNMR (Prediction of the Amount of Secondary Structure by Nuclear Magnetic Resonance), which can be accessed directly from the Internet. PASSNMR program is a powerful tool for screening proteins for proteomic or structural genomic investigations when used with recent methodologies that take advantage of the use of the antibiotic rifampicin to selectively label the heterologous proteins expressed in E. coli. PASSNMR analysis can be useful as a first approach to predict the amount of secondary structure in proteins to structural genomics. Information about the secondary structure of proteins can be obtained even before protein purification, with small quantities of protein, just by performing two simple nuclear magnetic resonance (NMR) experiments and using PASSNMR program. |
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Genetics and Molecular Biology |
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Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomicschemical shift dispersionPASSNMRprediction of secondary structurestructural proteomicstarget selectionWith the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13C, 15N and ¹H chemical shift dispersion to predict the amount of secondary structure of unassigned proteins from their 15N- and/or 13C-edited heteronuclear single quantum coherence (HSQC) spectra. This methodology has been coded into a software called PASSNMR (Prediction of the Amount of Secondary Structure by Nuclear Magnetic Resonance), which can be accessed directly from the Internet. PASSNMR program is a powerful tool for screening proteins for proteomic or structural genomic investigations when used with recent methodologies that take advantage of the use of the antibiotic rifampicin to selectively label the heterologous proteins expressed in E. coli. PASSNMR analysis can be useful as a first approach to predict the amount of secondary structure in proteins to structural genomics. Information about the secondary structure of proteins can be obtained even before protein purification, with small quantities of protein, just by performing two simple nuclear magnetic resonance (NMR) experiments and using PASSNMR program.Sociedade Brasileira de Genética2006-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030Genetics and Molecular Biology v.29 n.4 2006reponame:Genetics and Molecular Biologyinstname:Sociedade Brasileira de Genética (SBG)instacron:SBG10.1590/S1415-47572006000400030info:eu-repo/semantics/openAccessMoreau,Vitor HugoValente,Ana PaulaAlmeida,Fábio C.L.eng2006-11-21T00:00:00Zoai:scielo:S1415-47572006000400030Revistahttp://www.gmb.org.br/ONGhttps://old.scielo.br/oai/scielo-oai.php||editor@gmb.org.br1678-46851415-4757opendoar:2006-11-21T00:00Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG)false |
dc.title.none.fl_str_mv |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
title |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
spellingShingle |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics Moreau,Vitor Hugo chemical shift dispersion PASSNMR prediction of secondary structure structural proteomics target selection |
title_short |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
title_full |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
title_fullStr |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
title_full_unstemmed |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
title_sort |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
author |
Moreau,Vitor Hugo |
author_facet |
Moreau,Vitor Hugo Valente,Ana Paula Almeida,Fábio C.L. |
author_role |
author |
author2 |
Valente,Ana Paula Almeida,Fábio C.L. |
author2_role |
author author |
dc.contributor.author.fl_str_mv |
Moreau,Vitor Hugo Valente,Ana Paula Almeida,Fábio C.L. |
dc.subject.por.fl_str_mv |
chemical shift dispersion PASSNMR prediction of secondary structure structural proteomics target selection |
topic |
chemical shift dispersion PASSNMR prediction of secondary structure structural proteomics target selection |
description |
With the advent of structural genomics, the need for fast structural information about unknown proteins has increased. We describe a new methodology, based on 13C, 15N and ¹H chemical shift dispersion to predict the amount of secondary structure of unassigned proteins from their 15N- and/or 13C-edited heteronuclear single quantum coherence (HSQC) spectra. This methodology has been coded into a software called PASSNMR (Prediction of the Amount of Secondary Structure by Nuclear Magnetic Resonance), which can be accessed directly from the Internet. PASSNMR program is a powerful tool for screening proteins for proteomic or structural genomic investigations when used with recent methodologies that take advantage of the use of the antibiotic rifampicin to selectively label the heterologous proteins expressed in E. coli. PASSNMR analysis can be useful as a first approach to predict the amount of secondary structure in proteins to structural genomics. Information about the secondary structure of proteins can be obtained even before protein purification, with small quantities of protein, just by performing two simple nuclear magnetic resonance (NMR) experiments and using PASSNMR program. |
publishDate |
2006 |
dc.date.none.fl_str_mv |
2006-01-01 |
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=S1415-47572006000400030 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1415-47572006000400030 |
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 |
Sociedade Brasileira de Genética |
publisher.none.fl_str_mv |
Sociedade Brasileira de Genética |
dc.source.none.fl_str_mv |
Genetics and Molecular Biology v.29 n.4 2006 reponame:Genetics and Molecular Biology instname:Sociedade Brasileira de Genética (SBG) instacron:SBG |
instname_str |
Sociedade Brasileira de Genética (SBG) |
instacron_str |
SBG |
institution |
SBG |
reponame_str |
Genetics and Molecular Biology |
collection |
Genetics and Molecular Biology |
repository.name.fl_str_mv |
Genetics and Molecular Biology - Sociedade Brasileira de Genética (SBG) |
repository.mail.fl_str_mv |
||editor@gmb.org.br |
_version_ |
1752122380280397824 |