The Design of Repeat Proteins: Stability Conflicts with Functionality

Autores
Espada, Rocío; Ferreiro, Diego; Parra, Rodrigo Gonzalo
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces that are not conserved along members of the same family but specific for each interacting pair. These proteins have been extensively used as scaffolds for protein design that are usually centered on the maximization of the stability of the repeat arrays. Although overall stability is important for obtaining molecules with enhanced solubility and expression, natural occurring repeatproteins have unstable characteristics that are relevant for their binding properties. Here we discuss the state of the art for repeat protein designs and the ideas of allowing energetic conflicts for introducing enhanced functionality in the arrays.
Fil: Espada, Rocío. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Parra, Rodrigo Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Max Planck Institute For Biophysical Chemistry; Alemania
Materia
Repeat proteins
Protein folding
Designed proteins
Protein stability
Local frustration
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:11336/55433
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The Design of Repeat Proteins: Stability Conflicts with FunctionalityEspada, RocíoFerreiro, DiegoParra, Rodrigo GonzaloRepeat proteinsProtein foldingDesigned proteinsProtein stabilityLocal frustrationhttps://purl.org/becyt/ford/1.2https://purl.org/becyt/ford/1Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces that are not conserved along members of the same family but specific for each interacting pair. These proteins have been extensively used as scaffolds for protein design that are usually centered on the maximization of the stability of the repeat arrays. Although overall stability is important for obtaining molecules with enhanced solubility and expression, natural occurring repeatproteins have unstable characteristics that are relevant for their binding properties. Here we discuss the state of the art for repeat protein designs and the ideas of allowing energetic conflicts for introducing enhanced functionality in the arrays.Fil: Espada, Rocío. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Parra, Rodrigo Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Max Planck Institute For Biophysical Chemistry; AlemaniaInsight Medical Publishing2017-03info: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/11336/55433Espada, Rocío; Ferreiro, Diego; Parra, Rodrigo Gonzalo; The Design of Repeat Proteins: Stability Conflicts with Functionality; Insight Medical Publishing; Biochemistry & Molecular Biology Journal; 3; 1; 3-2017; 1-52471-8084CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.21767/2471-8084.100031info:eu-repo/semantics/altIdentifier/url/http://biochem-molbio.imedpub.com/the-design-of-repeat-proteins-stability-conflicts-with-functionality.php?aid=18884info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:27:38Zoai:ri.conicet.gov.ar:11336/55433instacron: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:34982025-10-15 14:27:38.802CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Design of Repeat Proteins: Stability Conflicts with Functionality
title The Design of Repeat Proteins: Stability Conflicts with Functionality
spellingShingle The Design of Repeat Proteins: Stability Conflicts with Functionality
Espada, Rocío
Repeat proteins
Protein folding
Designed proteins
Protein stability
Local frustration
title_short The Design of Repeat Proteins: Stability Conflicts with Functionality
title_full The Design of Repeat Proteins: Stability Conflicts with Functionality
title_fullStr The Design of Repeat Proteins: Stability Conflicts with Functionality
title_full_unstemmed The Design of Repeat Proteins: Stability Conflicts with Functionality
title_sort The Design of Repeat Proteins: Stability Conflicts with Functionality
dc.creator.none.fl_str_mv Espada, Rocío
Ferreiro, Diego
Parra, Rodrigo Gonzalo
author Espada, Rocío
author_facet Espada, Rocío
Ferreiro, Diego
Parra, Rodrigo Gonzalo
author_role author
author2 Ferreiro, Diego
Parra, Rodrigo Gonzalo
author2_role author
author
dc.subject.none.fl_str_mv Repeat proteins
Protein folding
Designed proteins
Protein stability
Local frustration
topic Repeat proteins
Protein folding
Designed proteins
Protein stability
Local frustration
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.2
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces that are not conserved along members of the same family but specific for each interacting pair. These proteins have been extensively used as scaffolds for protein design that are usually centered on the maximization of the stability of the repeat arrays. Although overall stability is important for obtaining molecules with enhanced solubility and expression, natural occurring repeatproteins have unstable characteristics that are relevant for their binding properties. Here we discuss the state of the art for repeat protein designs and the ideas of allowing energetic conflicts for introducing enhanced functionality in the arrays.
Fil: Espada, Rocío. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Ferreiro, Diego. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Parra, Rodrigo Gonzalo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina. Max Planck Institute For Biophysical Chemistry; Alemania
description Repeat proteins are constituted by a variable number of copies of a given structural element that is tandemly repeated along a longitudinal axis. They mainly function as protein-protein interactors with binding interfaces that are not conserved along members of the same family but specific for each interacting pair. These proteins have been extensively used as scaffolds for protein design that are usually centered on the maximization of the stability of the repeat arrays. Although overall stability is important for obtaining molecules with enhanced solubility and expression, natural occurring repeatproteins have unstable characteristics that are relevant for their binding properties. Here we discuss the state of the art for repeat protein designs and the ideas of allowing energetic conflicts for introducing enhanced functionality in the arrays.
publishDate 2017
dc.date.none.fl_str_mv 2017-03
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/11336/55433
Espada, Rocío; Ferreiro, Diego; Parra, Rodrigo Gonzalo; The Design of Repeat Proteins: Stability Conflicts with Functionality; Insight Medical Publishing; Biochemistry & Molecular Biology Journal; 3; 1; 3-2017; 1-5
2471-8084
CONICET Digital
CONICET
url http://hdl.handle.net/11336/55433
identifier_str_mv Espada, Rocío; Ferreiro, Diego; Parra, Rodrigo Gonzalo; The Design of Repeat Proteins: Stability Conflicts with Functionality; Insight Medical Publishing; Biochemistry & Molecular Biology Journal; 3; 1; 3-2017; 1-5
2471-8084
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.21767/2471-8084.100031
info:eu-repo/semantics/altIdentifier/url/http://biochem-molbio.imedpub.com/the-design-of-repeat-proteins-stability-conflicts-with-functionality.php?aid=18884
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 Insight Medical Publishing
publisher.none.fl_str_mv Insight Medical Publishing
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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score 13.22299

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