Evolutionary Conservation of Protein Backbone Flexibility

Autores
Maguid, Sandra; Fernández Alberti, Sebastián; Parisi, Gustavo Daniel; Echave, Julián
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Internal protein dynamics is essential for biological function. During evolution, protein divergence is functionally constrained: properties more relevant for function vary more slowly than less important properties. Thus, if protein dynamics is relevant for function, it should be evolutionary conserved. In contrast with the well-studied evolution of protein structure, the evolutionary divergence of protein dynamics has not been addressed systematically before, apart from a few case studies. X-Ray diffraction analysis gives information not only on protein structure but also on B-factors, which characterize the flexibility that results from protein dynamics. Here we study the evolutionary divergence of protein backbone dynamics by comparing the Cα flexibility (B-factor) profiles for a large dataset of homologous proteins classified into families and superfamilies. We show that Cα flexibility profiles diverge slowly, so that they are conserved at family and superfamily levels, even for pairs of proteins with nonsignificant sequence similarity. We also analyze and discuss the correlations among the divergences of flexibility, sequence, and structure.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/132816

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network_name_str SEDICI (UNLP)
spelling Evolutionary Conservation of Protein Backbone FlexibilityMaguid, SandraFernández Alberti, SebastiánParisi, Gustavo DanielEchave, JuliánCiencias ExactasQuímicaFlexibility profilesProtein dynamicsProtein evolutionInternal protein dynamics is essential for biological function. During evolution, protein divergence is functionally constrained: properties more relevant for function vary more slowly than less important properties. Thus, if protein dynamics is relevant for function, it should be evolutionary conserved. In contrast with the well-studied evolution of protein structure, the evolutionary divergence of protein dynamics has not been addressed systematically before, apart from a few case studies. X-Ray diffraction analysis gives information not only on protein structure but also on B-factors, which characterize the flexibility that results from protein dynamics. Here we study the evolutionary divergence of protein backbone dynamics by comparing the Cα flexibility (B-factor) profiles for a large dataset of homologous proteins classified into families and superfamilies. We show that Cα flexibility profiles diverge slowly, so that they are conserved at family and superfamily levels, even for pairs of proteins with nonsignificant sequence similarity. We also analyze and discuss the correlations among the divergences of flexibility, sequence, and structure.Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2006-10-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf448-457http://sedici.unlp.edu.ar/handle/10915/132816enginfo:eu-repo/semantics/altIdentifier/issn/0022-2844info:eu-repo/semantics/altIdentifier/issn/1432-1432info:eu-repo/semantics/altIdentifier/doi/10.1007/s00239-005-0209-xinfo:eu-repo/semantics/altIdentifier/pmid/17021932info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:31:43Zoai:sedici.unlp.edu.ar:10915/132816Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:31:43.526SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Evolutionary Conservation of Protein Backbone Flexibility
title Evolutionary Conservation of Protein Backbone Flexibility
spellingShingle Evolutionary Conservation of Protein Backbone Flexibility
Maguid, Sandra
Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
title_short Evolutionary Conservation of Protein Backbone Flexibility
title_full Evolutionary Conservation of Protein Backbone Flexibility
title_fullStr Evolutionary Conservation of Protein Backbone Flexibility
title_full_unstemmed Evolutionary Conservation of Protein Backbone Flexibility
title_sort Evolutionary Conservation of Protein Backbone Flexibility
dc.creator.none.fl_str_mv Maguid, Sandra
Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
author Maguid, Sandra
author_facet Maguid, Sandra
Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
author_role author
author2 Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
topic Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
dc.description.none.fl_txt_mv Internal protein dynamics is essential for biological function. During evolution, protein divergence is functionally constrained: properties more relevant for function vary more slowly than less important properties. Thus, if protein dynamics is relevant for function, it should be evolutionary conserved. In contrast with the well-studied evolution of protein structure, the evolutionary divergence of protein dynamics has not been addressed systematically before, apart from a few case studies. X-Ray diffraction analysis gives information not only on protein structure but also on B-factors, which characterize the flexibility that results from protein dynamics. Here we study the evolutionary divergence of protein backbone dynamics by comparing the Cα flexibility (B-factor) profiles for a large dataset of homologous proteins classified into families and superfamilies. We show that Cα flexibility profiles diverge slowly, so that they are conserved at family and superfamily levels, even for pairs of proteins with nonsignificant sequence similarity. We also analyze and discuss the correlations among the divergences of flexibility, sequence, and structure.
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description Internal protein dynamics is essential for biological function. During evolution, protein divergence is functionally constrained: properties more relevant for function vary more slowly than less important properties. Thus, if protein dynamics is relevant for function, it should be evolutionary conserved. In contrast with the well-studied evolution of protein structure, the evolutionary divergence of protein dynamics has not been addressed systematically before, apart from a few case studies. X-Ray diffraction analysis gives information not only on protein structure but also on B-factors, which characterize the flexibility that results from protein dynamics. Here we study the evolutionary divergence of protein backbone dynamics by comparing the Cα flexibility (B-factor) profiles for a large dataset of homologous proteins classified into families and superfamilies. We show that Cα flexibility profiles diverge slowly, so that they are conserved at family and superfamily levels, even for pairs of proteins with nonsignificant sequence similarity. We also analyze and discuss the correlations among the divergences of flexibility, sequence, and structure.
publishDate 2006
dc.date.none.fl_str_mv 2006-10-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/132816
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dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0022-2844
info:eu-repo/semantics/altIdentifier/issn/1432-1432
info:eu-repo/semantics/altIdentifier/doi/10.1007/s00239-005-0209-x
info:eu-repo/semantics/altIdentifier/pmid/17021932
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
448-457
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instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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