Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins

Autores
RASIA, Rodolfo Maximiliano; Brutscher, Bernhard; Plevin, Michael J.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.
Fil: RASIA, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Brutscher, Bernhard. Centre National de la Recherche Scientifique; Francia
Fil: Plevin, Michael J.. Centre National de la Recherche Scientifique; Francia
Materia
Isotopic unlabeling
Hadamard Spectroscopy
Intrinsically disordered proteins
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/269473

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spelling Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered ProteinsRASIA, Rodolfo MaximilianoBrutscher, BernhardPlevin, Michael J.Isotopic unlabelingHadamard SpectroscopyIntrinsically disordered proteinshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.Fil: RASIA, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Brutscher, Bernhard. Centre National de la Recherche Scientifique; FranciaFil: Plevin, Michael J.. Centre National de la Recherche Scientifique; FranciaWiley VCH Verlag2012-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/269473RASIA, Rodolfo Maximiliano; Brutscher, Bernhard; Plevin, Michael J.; Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins; Wiley VCH Verlag; Chembiochem; 13; 5; 3-2012; 732-7391439-4227CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.201100678info:eu-repo/semantics/altIdentifier/doi/10.1002/cbic.201100678info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:45:57Zoai:ri.conicet.gov.ar:11336/269473instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:45:58.076CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
title Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
spellingShingle Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
RASIA, Rodolfo Maximiliano
Isotopic unlabeling
Hadamard Spectroscopy
Intrinsically disordered proteins
title_short Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
title_full Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
title_fullStr Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
title_full_unstemmed Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
title_sort Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins
dc.creator.none.fl_str_mv RASIA, Rodolfo Maximiliano
Brutscher, Bernhard
Plevin, Michael J.
author RASIA, Rodolfo Maximiliano
author_facet RASIA, Rodolfo Maximiliano
Brutscher, Bernhard
Plevin, Michael J.
author_role author
author2 Brutscher, Bernhard
Plevin, Michael J.
author2_role author
author
dc.subject.none.fl_str_mv Isotopic unlabeling
Hadamard Spectroscopy
Intrinsically disordered proteins
topic Isotopic unlabeling
Hadamard Spectroscopy
Intrinsically disordered proteins
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.
Fil: RASIA, Rodolfo Maximiliano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Biología Molecular y Celular de Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Brutscher, Bernhard. Centre National de la Recherche Scientifique; Francia
Fil: Plevin, Michael J.. Centre National de la Recherche Scientifique; Francia
description Selective isotopic unlabeling of proteins can provide important residue-type information as well as reduce congestion of NMR spectra. However, metabolic scrambling often complicates the final isotope-labeling pattern. Here, an array of metabolic precursors is used to perform robust, residue-specific unlabeling of proteins. The resulting isotopic-labeling patterns are predictable and nicely complement NMR experiments that differentiate residue types. This approach has widespread applications, but it is particularly relevant for proteins that lack sequence complexity or a defined tertiary structure.
publishDate 2012
dc.date.none.fl_str_mv 2012-03
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/269473
RASIA, Rodolfo Maximiliano; Brutscher, Bernhard; Plevin, Michael J.; Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins; Wiley VCH Verlag; Chembiochem; 13; 5; 3-2012; 732-739
1439-4227
CONICET Digital
CONICET
url http://hdl.handle.net/11336/269473
identifier_str_mv RASIA, Rodolfo Maximiliano; Brutscher, Bernhard; Plevin, Michael J.; Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins; Wiley VCH Verlag; Chembiochem; 13; 5; 3-2012; 732-739
1439-4227
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.201100678
info:eu-repo/semantics/altIdentifier/doi/10.1002/cbic.201100678
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Wiley VCH Verlag
publisher.none.fl_str_mv Wiley VCH Verlag
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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