Long-lived States in an intrinsically disordered protein domain

Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is disordered in vitro under physiological conditio...

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Detalles Bibliográficos
Autores: Fernandes, L., Guerniou, C., Marín Montesinos, Ildefonso, Pons Vallès, Miquel, Kateb, F., Vasos, P. R.
Tipo de recurso: artículo
Estado:Versión enviada para evaluación y publicación
Fecha de publicación:2013
País:España
Institución:Universidad de Barcelona
Repositorio:Dipòsit Digital de la UB
OAI Identifier:oai:diposit.ub.edu:2445/47994
Acceso en línea:https://hdl.handle.net/2445/47994
Access Level:acceso abierto
Palabra clave:Espectroscòpia de ressonància magnètica nuclear
Spin (Física nuclear)
Relaxació (Física nuclear)
Proteïnes quinases
Bioquímica
Nuclear magnetic resonance spectroscopy
Nuclear spin
Relaxation (Nuclear physics)
Protein kinases
Biochemistry
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repository_id_str
spelling Long-lived States in an intrinsically disordered protein domainFernandes, L.Guerniou, C.Marín Montesinos, IldefonsoPons Vallès, MiquelKateb, F.Vasos, P. R.Espectroscòpia de ressonància magnètica nuclearSpin (Física nuclear)Relaxació (Física nuclear)Proteïnes quinasesBioquímicaNuclear magnetic resonance spectroscopyNuclear spinRelaxation (Nuclear physics)Protein kinasesBiochemistryLong-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is disordered in vitro under physiological conditions. The relaxation rates of LLS are a probe for motions and interactions in biomolecules. LLS of the aliphatic protons of glycines, with lifetimes ca. four times longer than their spin-lattice relaxation times, are reported for the first time in an intrinsically disordered protein domain (IDP). LLS relaxation experiments were integrated with 2D spectroscopy methods, further adapting them for studies on proteins.John Wiley & Sons2013info:eu-repo/semantics/articleinfo:eu-repo/semantics/submittedVersionapplication/pdfhttps://hdl.handle.net/2445/47994Articles publicats en revistes (Química Inorgànica i Orgànica)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésVersió preprint del document publicat a: http://dx.doi.org/10.1002/mrc.4008Magnetic Resonance in Chemistry, 2013, vol. 51, p. 729-733http://dx.doi.org/10.1002/mrc.4008(c) John Wiley & Sons, 2013info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/479942026-05-27T06:46:51Z
dc.title.none.fl_str_mv Long-lived States in an intrinsically disordered protein domain
title Long-lived States in an intrinsically disordered protein domain
spellingShingle Long-lived States in an intrinsically disordered protein domain
Fernandes, L.
Espectroscòpia de ressonància magnètica nuclear
Spin (Física nuclear)
Relaxació (Física nuclear)
Proteïnes quinases
Bioquímica
Nuclear magnetic resonance spectroscopy
Nuclear spin
Relaxation (Nuclear physics)
Protein kinases
Biochemistry
title_short Long-lived States in an intrinsically disordered protein domain
title_full Long-lived States in an intrinsically disordered protein domain
title_fullStr Long-lived States in an intrinsically disordered protein domain
title_full_unstemmed Long-lived States in an intrinsically disordered protein domain
title_sort Long-lived States in an intrinsically disordered protein domain
dc.creator.none.fl_str_mv Fernandes, L.
Guerniou, C.
Marín Montesinos, Ildefonso
Pons Vallès, Miquel
Kateb, F.
Vasos, P. R.
author Fernandes, L.
author_facet Fernandes, L.
Guerniou, C.
Marín Montesinos, Ildefonso
Pons Vallès, Miquel
Kateb, F.
Vasos, P. R.
author_role author
author2 Guerniou, C.
Marín Montesinos, Ildefonso
Pons Vallès, Miquel
Kateb, F.
Vasos, P. R.
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Espectroscòpia de ressonància magnètica nuclear
Spin (Física nuclear)
Relaxació (Física nuclear)
Proteïnes quinases
Bioquímica
Nuclear magnetic resonance spectroscopy
Nuclear spin
Relaxation (Nuclear physics)
Protein kinases
Biochemistry
topic Espectroscòpia de ressonància magnètica nuclear
Spin (Física nuclear)
Relaxació (Física nuclear)
Proteïnes quinases
Bioquímica
Nuclear magnetic resonance spectroscopy
Nuclear spin
Relaxation (Nuclear physics)
Protein kinases
Biochemistry
description Long-lived states (LLS) are relaxation-favoured eigenstates of J-coupled magnetic nuclei. LLS were measured, along with classical 1H and 15 N relaxation rate constants, in aminoacids of the N-terminal Unique domain of the c-Src kinase (USrc), which is disordered in vitro under physiological conditions. The relaxation rates of LLS are a probe for motions and interactions in biomolecules. LLS of the aliphatic protons of glycines, with lifetimes ca. four times longer than their spin-lattice relaxation times, are reported for the first time in an intrinsically disordered protein domain (IDP). LLS relaxation experiments were integrated with 2D spectroscopy methods, further adapting them for studies on proteins.
publishDate 2013
dc.date.none.fl_str_mv 2013
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/submittedVersion
format article
status_str submittedVersion
dc.identifier.none.fl_str_mv https://hdl.handle.net/2445/47994
url https://hdl.handle.net/2445/47994
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv Versió preprint del document publicat a: http://dx.doi.org/10.1002/mrc.4008
Magnetic Resonance in Chemistry, 2013, vol. 51, p. 729-733
http://dx.doi.org/10.1002/mrc.4008
dc.rights.none.fl_str_mv (c) John Wiley & Sons, 2013
info:eu-repo/semantics/openAccess
rights_invalid_str_mv (c) John Wiley & Sons, 2013
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv John Wiley & Sons
publisher.none.fl_str_mv John Wiley & Sons
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 15,300719

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