CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state

Autores
Monzón, Alexander; Rohr, Cristian Oscar; Fornasari, Maria Silvina; Parisi, Gustavo Daniel
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
CoDNaS (conformational diversity of the native state) is a protein conformational diversitydatabase. Conformational diversity describes structural differences between conformersthat define the native state of proteins. It is a key concept to understand proteinfunction and biological processes related to protein functions. CoDNaS offers a well curateddatabase that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitatesthe extraction of key information on small structural differences based on proteinmovements. CoDNaS enables users to easily relate the degree of conformational diversitywith physical, chemical and biological properties derived from experiments on proteinstructure and biological characteristics. The new version of CoDNaS includes 70%of all available protein structures, and new tools have been added that run sequencesearches, display structural flexibility profiles and allow users to browse the database fordifferent structural classes. These tools facilitate the exploration of protein conformationaldiversity and its role in protein function.
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Rohr, Cristian Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Ecología, Genética y Evolución de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Ecología, Genética y Evolución de Buenos Aires; Argentina
Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Materia
Databases
Conformational Diversity
Protein
Bioinformatics
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/40550
Acceder
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network_name_str CONICET Digital (CONICET)
spelling CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native stateMonzón, AlexanderRohr, Cristian OscarFornasari, Maria SilvinaParisi, Gustavo DanielDatabasesConformational DiversityProteinBioinformaticshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1CoDNaS (conformational diversity of the native state) is a protein conformational diversitydatabase. Conformational diversity describes structural differences between conformersthat define the native state of proteins. It is a key concept to understand proteinfunction and biological processes related to protein functions. CoDNaS offers a well curateddatabase that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitatesthe extraction of key information on small structural differences based on proteinmovements. CoDNaS enables users to easily relate the degree of conformational diversitywith physical, chemical and biological properties derived from experiments on proteinstructure and biological characteristics. The new version of CoDNaS includes 70%of all available protein structures, and new tools have been added that run sequencesearches, display structural flexibility profiles and allow users to browse the database fordifferent structural classes. These tools facilitate the exploration of protein conformationaldiversity and its role in protein function.Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Rohr, Cristian Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Ecología, Genética y Evolución de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Ecología, Genética y Evolución de Buenos Aires; ArgentinaFil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaFil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; ArgentinaOxford Journal2016-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/40550Monzón, Alexander; Rohr, Cristian Oscar; Fornasari, Maria Silvina; Parisi, Gustavo Daniel; CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state; Oxford Journal; Database: the journal of biological databases and curation; 2016; 3-2016; 1-81758-0463CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1093/database/baw038info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/database/article/doi/10.1093/database/baw038/2630306info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:17:59Zoai:ri.conicet.gov.ar:11336/40550instacron: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 10:17:59.242CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
title CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
spellingShingle CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
Monzón, Alexander
Databases
Conformational Diversity
Protein
Bioinformatics
title_short CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
title_full CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
title_fullStr CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
title_full_unstemmed CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
title_sort CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state
dc.creator.none.fl_str_mv Monzón, Alexander
Rohr, Cristian Oscar
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author Monzón, Alexander
author_facet Monzón, Alexander
Rohr, Cristian Oscar
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author_role author
author2 Rohr, Cristian Oscar
Fornasari, Maria Silvina
Parisi, Gustavo Daniel
author2_role author
author
author
dc.subject.none.fl_str_mv Databases
Conformational Diversity
Protein
Bioinformatics
topic Databases
Conformational Diversity
Protein
Bioinformatics
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv CoDNaS (conformational diversity of the native state) is a protein conformational diversitydatabase. Conformational diversity describes structural differences between conformersthat define the native state of proteins. It is a key concept to understand proteinfunction and biological processes related to protein functions. CoDNaS offers a well curateddatabase that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitatesthe extraction of key information on small structural differences based on proteinmovements. CoDNaS enables users to easily relate the degree of conformational diversitywith physical, chemical and biological properties derived from experiments on proteinstructure and biological characteristics. The new version of CoDNaS includes 70%of all available protein structures, and new tools have been added that run sequencesearches, display structural flexibility profiles and allow users to browse the database fordifferent structural classes. These tools facilitate the exploration of protein conformationaldiversity and its role in protein function.
Fil: Monzón, Alexander. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Rohr, Cristian Oscar. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Ecología, Genética y Evolución de Buenos Aires. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Ecología, Genética y Evolución de Buenos Aires; Argentina
Fil: Fornasari, Maria Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
Fil: Parisi, Gustavo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología; Argentina
description CoDNaS (conformational diversity of the native state) is a protein conformational diversitydatabase. Conformational diversity describes structural differences between conformersthat define the native state of proteins. It is a key concept to understand proteinfunction and biological processes related to protein functions. CoDNaS offers a well curateddatabase that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitatesthe extraction of key information on small structural differences based on proteinmovements. CoDNaS enables users to easily relate the degree of conformational diversitywith physical, chemical and biological properties derived from experiments on proteinstructure and biological characteristics. The new version of CoDNaS includes 70%of all available protein structures, and new tools have been added that run sequencesearches, display structural flexibility profiles and allow users to browse the database fordifferent structural classes. These tools facilitate the exploration of protein conformationaldiversity and its role in protein function.
publishDate 2016
dc.date.none.fl_str_mv 2016-03
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/11336/40550
Monzón, Alexander; Rohr, Cristian Oscar; Fornasari, Maria Silvina; Parisi, Gustavo Daniel; CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state; Oxford Journal; Database: the journal of biological databases and curation; 2016; 3-2016; 1-8
1758-0463
CONICET Digital
CONICET
url http://hdl.handle.net/11336/40550
identifier_str_mv Monzón, Alexander; Rohr, Cristian Oscar; Fornasari, Maria Silvina; Parisi, Gustavo Daniel; CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state; Oxford Journal; Database: the journal of biological databases and curation; 2016; 3-2016; 1-8
1758-0463
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1093/database/baw038
info:eu-repo/semantics/altIdentifier/url/https://academic.oup.com/database/article/doi/10.1093/database/baw038/2630306
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Oxford Journal
publisher.none.fl_str_mv Oxford Journal
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 13.070432

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