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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/55433
Ver los metadatos del registro completo
id |
CONICETDig_fd095ba3e7f824749e6cacc80c472c7d |
---|---|
oai_identifier_str |
oai:ri.conicet.gov.ar:11336/55433 |
network_acronym_str |
CONICETDig |
repository_id_str |
3498 |
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 Técnicas2025-09-29T09:38:27Zoai: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:34982025-09-29 09:38:27.439CONICET 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 |
_version_ |
1844613215473893376 |
score |
13.070432 |