Evolutionary Conservation of Protein Backbone Flexibility

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 conse...

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Detalles Bibliográficos
Autores principales: Maguid, Sandra, Fernández Alberti, Sebastián, Parisi, Gustavo Daniel, Echave, Julián
Formato: Articulo
Lenguaje:Inglés
Publicado: 2006
Materias:
Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/132816
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-132816
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Inglés
topic Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
spellingShingle Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
Maguid, Sandra
Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
Evolutionary Conservation of Protein Backbone Flexibility
topic_facet Ciencias Exactas
Química
Flexibility profiles
Protein dynamics
Protein evolution
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.
format Articulo
Articulo
author Maguid, Sandra
Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
author_facet Maguid, Sandra
Fernández Alberti, Sebastián
Parisi, Gustavo Daniel
Echave, Julián
author_sort Maguid, Sandra
title Evolutionary Conservation of Protein Backbone Flexibility
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
publishDate 2006
url http://sedici.unlp.edu.ar/handle/10915/132816
work_keys_str_mv AT maguidsandra evolutionaryconservationofproteinbackboneflexibility
AT fernandezalbertisebastian evolutionaryconservationofproteinbackboneflexibility
AT parisigustavodaniel evolutionaryconservationofproteinbackboneflexibility
AT echavejulian evolutionaryconservationofproteinbackboneflexibility
bdutipo_str Repositorios
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