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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/132816
Ver los metadatos del registro completo
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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 |
url |
http://sedici.unlp.edu.ar/handle/10915/132816 |
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) |
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application/pdf 448-457 |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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