Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo

Nuclear Magnetic Resonance (NMR) spectroscopy has applications in multiple areas of science, especially in chemistry, biochemistry and biomedicine. NMR is a very versatile technique for determining the structure, dynamics and interactions of organic molecules and biomolecules in solution. Also, NMR...

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Detalhes bibliográficos
Autor: Serrano Serrano, Soraya
Formato: tesis doctoral
Fecha de publicación:2015
País:España
Recursos:Universidad Complutense de Madrid (UCM)
Repositorio:Docta Complutense
Idioma:español
OAI Identifier:oai:docta.ucm.es:20.500.14352/38646
Acesso em linha:https://hdl.handle.net/20.500.14352/38646
Access Level:acceso abierto
Palavra-chave:577.1(043.2)
Bioquímica
Biochemistry
Bioquímica (Química)
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spelling Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modeloSerrano Serrano, Soraya577.1(043.2)BioquímicaBiochemistryBioquímica (Química)Nuclear Magnetic Resonance (NMR) spectroscopy has applications in multiple areas of science, especially in chemistry, biochemistry and biomedicine. NMR is a very versatile technique for determining the structure, dynamics and interactions of organic molecules and biomolecules in solution. Also, NMR is a technique experimenting rapid and continuous advances, both by instrument technology and by the development of new experimental techniques. In this context, chapter II of this Thesis addresses the development of a new pulse sequence, which provides a new tool for the study of intrinsically disordered proteins (IDPs). This is of great relevance because of the complex conformational behavior of IDPs, and the increasing number of known IDPs. Meanwhile, chapters III-V exploit the NMR versatility for the characterization and structural determination of biomolecules and their interactions. Structural characterization and dynamics of these interactions with atomic resolution is essential to understand their functionality within the cell. This information can be of practical use, for instance, in the development of new drugs and new therapeutic strategies for the treatment of various diseases. Within this broad field, chapters III-IV aim to characterize the interactions of two particular biological systems using both protein and membrane mimetics. The two systems studied include boomerang peptides as heparin-binding models, in chapter III, and peptides derived from the gp41 protein in presence of simple mimetic of membrane environments, an apolar medium and micelles, in chapter IV. In chapter V, a complete characterization of a circularly permutated onconasa variant, ONCFLG zymogen, is performed. The internal dynamics and the conformational stability at the residue level are determined. The findings on these systems has provided us additional information to that available before starting this work, which allow us to derive structure-function implications. In brief, the work done in this Thesis has provided us a new experimental NMR method applicable to intrinsically disordered protein, an emerging area in the protein field, and new data about three biological systems, which has improved our understanding of the molecular basis of their biological functions.Universidad Complutense de MadridBruix Bayés, MartaJiménez López, María ÁngelesUniversidad Complutense de Madrid20152015-01-0120152015-01-01doctoral thesishttp://purl.org/coar/resource_type/c_db06info:eu-repo/semantics/doctoralThesisapplication/pdfhttps://hdl.handle.net/20.500.14352/38646reponame:Docta Complutenseinstname:Universidad Complutense de Madrid (UCM)Españolspaopen accesshttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessoai:docta.ucm.es:20.500.14352/386462026-06-02T12:44:21Z
dc.title.none.fl_str_mv Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
title Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
spellingShingle Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
Serrano Serrano, Soraya
577.1(043.2)
Bioquímica
Biochemistry
Bioquímica (Química)
title_short Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
title_full Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
title_fullStr Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
title_full_unstemmed Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
title_sort Interacciones proteína-membrana: una aproximación estructural por RMN utilizando sistemas modelo
dc.creator.none.fl_str_mv Serrano Serrano, Soraya
author Serrano Serrano, Soraya
author_facet Serrano Serrano, Soraya
author_role author
dc.contributor.none.fl_str_mv Bruix Bayés, Marta
Jiménez López, María Ángeles
Universidad Complutense de Madrid
dc.subject.none.fl_str_mv 577.1(043.2)
Bioquímica
Biochemistry
Bioquímica (Química)
topic 577.1(043.2)
Bioquímica
Biochemistry
Bioquímica (Química)
description Nuclear Magnetic Resonance (NMR) spectroscopy has applications in multiple areas of science, especially in chemistry, biochemistry and biomedicine. NMR is a very versatile technique for determining the structure, dynamics and interactions of organic molecules and biomolecules in solution. Also, NMR is a technique experimenting rapid and continuous advances, both by instrument technology and by the development of new experimental techniques. In this context, chapter II of this Thesis addresses the development of a new pulse sequence, which provides a new tool for the study of intrinsically disordered proteins (IDPs). This is of great relevance because of the complex conformational behavior of IDPs, and the increasing number of known IDPs. Meanwhile, chapters III-V exploit the NMR versatility for the characterization and structural determination of biomolecules and their interactions. Structural characterization and dynamics of these interactions with atomic resolution is essential to understand their functionality within the cell. This information can be of practical use, for instance, in the development of new drugs and new therapeutic strategies for the treatment of various diseases. Within this broad field, chapters III-IV aim to characterize the interactions of two particular biological systems using both protein and membrane mimetics. The two systems studied include boomerang peptides as heparin-binding models, in chapter III, and peptides derived from the gp41 protein in presence of simple mimetic of membrane environments, an apolar medium and micelles, in chapter IV. In chapter V, a complete characterization of a circularly permutated onconasa variant, ONCFLG zymogen, is performed. The internal dynamics and the conformational stability at the residue level are determined. The findings on these systems has provided us additional information to that available before starting this work, which allow us to derive structure-function implications. In brief, the work done in this Thesis has provided us a new experimental NMR method applicable to intrinsically disordered protein, an emerging area in the protein field, and new data about three biological systems, which has improved our understanding of the molecular basis of their biological functions.
publishDate 2015
dc.date.none.fl_str_mv 2015
2015-01-01
2015
2015-01-01
dc.type.none.fl_str_mv doctoral thesis
http://purl.org/coar/resource_type/c_db06
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format doctoralThesis
dc.identifier.none.fl_str_mv https://hdl.handle.net/20.500.14352/38646
url https://hdl.handle.net/20.500.14352/38646
dc.language.none.fl_str_mv Español
spa
language_invalid_str_mv Español
language spa
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Universidad Complutense de Madrid
publisher.none.fl_str_mv Universidad Complutense de Madrid
dc.source.none.fl_str_mv reponame:Docta Complutense
instname:Universidad Complutense de Madrid (UCM)
instname_str Universidad Complutense de Madrid (UCM)
reponame_str Docta Complutense
collection Docta Complutense
repository.name.fl_str_mv
repository.mail.fl_str_mv
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