Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics
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-edit...
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2006-01-01
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doaj-a15f8e9b6c06434f94343926f1fb68092020-11-24T21:33:39ZengSociedade Brasileira de GenéticaGenetics and Molecular Biology1415-47571678-46852006-01-0129476277010.1590/S1415-47572006000400030Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomicsVitor Hugo MoreauAna Paula ValenteFábio C.L. AlmeidaWith 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.http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030chemical shift dispersionPASSNMRprediction of secondary structurestructural proteomicstarget selection |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Vitor Hugo Moreau Ana Paula Valente Fábio C.L. Almeida |
spellingShingle |
Vitor Hugo Moreau Ana Paula Valente Fábio C.L. Almeida Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics Genetics and Molecular Biology chemical shift dispersion PASSNMR prediction of secondary structure structural proteomics target selection |
author_facet |
Vitor Hugo Moreau Ana Paula Valente Fábio C.L. Almeida |
author_sort |
Vitor Hugo Moreau |
title |
Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics |
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 |
publisher |
Sociedade Brasileira de Genética |
series |
Genetics and Molecular Biology |
issn |
1415-4757 1678-4685 |
publishDate |
2006-01-01 |
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. |
topic |
chemical shift dispersion PASSNMR prediction of secondary structure structural proteomics target selection |
url |
http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1415-47572006000400030 |
work_keys_str_mv |
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1725952838671007744 |