An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination

Dissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical o...

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Detalles Bibliográficos
Autores: Puig-Sàrries, Pilar, Bijlmakers, Marie-Jose, Zuin, Alice, Bichmann, Anne, Pons Vallès, Miquel, Crosas i Navarro, Bernat
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2015
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/138584
Acceso en línea:https://hdl.handle.net/2445/138584
Access Level:acceso abierto
Palabra clave:Ubiqüitina
Proteïnes
Ubiquitin
Proteins
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spelling An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitinationPuig-Sàrries, PilarBijlmakers, Marie-JoseZuin, AliceBichmann, AnnePons Vallès, MiquelCrosas i Navarro, BernatUbiqüitinaProteïnesUbiquitinProteinsDissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical optimizations in order to use dissolution DNP for biochemical and chemical applications. Here we show how a newly designed pressure dissolution kit considerably improves spectral quality and stability by enabling highly reliable and fast sample transfer to the NMR system.Biochemical Society2015info:eu-repo/semantics/articleinfo:eu-repo/semantics/acceptedVersionapplication/pdfhttps://hdl.handle.net/2445/138584Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésVersió postprint del document publicat a: https://doi.org/10.1042/BJ20141571Biochemical Journal, 2015, vol. 469, num. 3, p. 455-467https://doi.org/10.1042/BJ20141571(c) Puig-Sàrries, Pilar et al., 2015info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1385842026-05-27T06:46:51Z
dc.title.none.fl_str_mv An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
title An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
spellingShingle An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
Puig-Sàrries, Pilar
Ubiqüitina
Proteïnes
Ubiquitin
Proteins
title_short An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
title_full An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
title_fullStr An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
title_full_unstemmed An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
title_sort An intrinsically disordered region of RPN10 plays a key role in restricting ubiquitin chain elongation in RPN10 monoubiquitination
dc.creator.none.fl_str_mv Puig-Sàrries, Pilar
Bijlmakers, Marie-Jose
Zuin, Alice
Bichmann, Anne
Pons Vallès, Miquel
Crosas i Navarro, Bernat
author Puig-Sàrries, Pilar
author_facet Puig-Sàrries, Pilar
Bijlmakers, Marie-Jose
Zuin, Alice
Bichmann, Anne
Pons Vallès, Miquel
Crosas i Navarro, Bernat
author_role author
author2 Bijlmakers, Marie-Jose
Zuin, Alice
Bichmann, Anne
Pons Vallès, Miquel
Crosas i Navarro, Bernat
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ubiqüitina
Proteïnes
Ubiquitin
Proteins
topic Ubiqüitina
Proteïnes
Ubiquitin
Proteins
description Dissolution dynamic nuclear polarization (DNP) has become one of the predominant implementations for DNP. However, the technical implementation of transferring the sample from the polarizer to the nuclear magnetic resonance (NMR) system remains challenging. There is a need for additional technical optimizations in order to use dissolution DNP for biochemical and chemical applications. Here we show how a newly designed pressure dissolution kit considerably improves spectral quality and stability by enabling highly reliable and fast sample transfer to the NMR system.
publishDate 2015
dc.date.none.fl_str_mv 2015
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/138584
url https://hdl.handle.net/2445/138584
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió postprint del document publicat a: https://doi.org/10.1042/BJ20141571
Biochemical Journal, 2015, vol. 469, num. 3, p. 455-467
https://doi.org/10.1042/BJ20141571
dc.rights.none.fl_str_mv (c) Puig-Sàrries, Pilar et al., 2015
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) Puig-Sàrries, Pilar et al., 2015
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Biochemical Society
publisher.none.fl_str_mv Biochemical Society
dc.source.none.fl_str_mv Articles publicats en revistes (Química Inorgànica i Orgànica)
reponame:Dipòsit Digital de la UB
instname:Universidad de Barcelona
instname_str Universidad de Barcelona
reponame_str Dipòsit Digital de la UB
collection Dipòsit Digital de la UB
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,301629

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