Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence

Autores
Echave, Julian; Wilke, Claus O.
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
For decades, rates of protein evolution have been interpreted in terms of the vague concept of “functional importance”. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic mis-folding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field.
Fil: Echave, Julian. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
Materia
EVOLUTIONARY RATE
FITNESS LANDSCAPE
PROTEIN FOLDING
PROTEIN MISFOLDING
PROTEIN-PROTEIN INTERACTION
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/199789

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spelling Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence DivergenceEchave, JulianWilke, Claus O.EVOLUTIONARY RATEFITNESS LANDSCAPEPROTEIN FOLDINGPROTEIN MISFOLDINGPROTEIN-PROTEIN INTERACTIONhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1For decades, rates of protein evolution have been interpreted in terms of the vague concept of “functional importance”. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic mis-folding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field.Fil: Echave, Julian. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Wilke, Claus O.. University of Texas at Austin; Estados UnidosAnnual Reviews2017-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/199789Echave, Julian; Wilke, Claus O.; Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence; Annual Reviews; Annual Review Of Biophysics; 46; 5-2017; 85-1031936-122X1936-1238CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.annualreviews.org/doi/10.1146/annurev-biophys-070816-033819info:eu-repo/semantics/altIdentifier/doi/10.1146/annurev-biophys-070816-033819info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:03:59Zoai:ri.conicet.gov.ar:11336/199789instacron: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 10:03:59.337CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
title Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
spellingShingle Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
Echave, Julian
EVOLUTIONARY RATE
FITNESS LANDSCAPE
PROTEIN FOLDING
PROTEIN MISFOLDING
PROTEIN-PROTEIN INTERACTION
title_short Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
title_full Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
title_fullStr Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
title_full_unstemmed Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
title_sort Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence
dc.creator.none.fl_str_mv Echave, Julian
Wilke, Claus O.
author Echave, Julian
author_facet Echave, Julian
Wilke, Claus O.
author_role author
author2 Wilke, Claus O.
author2_role author
dc.subject.none.fl_str_mv EVOLUTIONARY RATE
FITNESS LANDSCAPE
PROTEIN FOLDING
PROTEIN MISFOLDING
PROTEIN-PROTEIN INTERACTION
topic EVOLUTIONARY RATE
FITNESS LANDSCAPE
PROTEIN FOLDING
PROTEIN MISFOLDING
PROTEIN-PROTEIN INTERACTION
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv For decades, rates of protein evolution have been interpreted in terms of the vague concept of “functional importance”. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic mis-folding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field.
Fil: Echave, Julian. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
description For decades, rates of protein evolution have been interpreted in terms of the vague concept of “functional importance”. Slowly evolving proteins or sites within proteins were assumed to be more functionally important and thus subject to stronger selection pressure. More recently, biophysical models of protein evolution, which combine evolutionary theory with protein biophysics, have completely revolutionized our view of the forces that shape sequence divergence. Slowly evolving proteins have been found to evolve slowly because of selection against toxic mis-folding and misinteractions, linking their rate of evolution primarily to their abundance. Similarly, most slowly evolving sites in proteins are not directly involved in function, but mutating them has large impacts on protein structure and stability. Here, we review the studies of the emergent field of biophysical protein evolution that have shaped our current understanding of sequence divergence patterns. We also propose future research directions to develop this nascent field.
publishDate 2017
dc.date.none.fl_str_mv 2017-05
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/11336/199789
Echave, Julian; Wilke, Claus O.; Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence; Annual Reviews; Annual Review Of Biophysics; 46; 5-2017; 85-103
1936-122X
1936-1238
CONICET Digital
CONICET
url http://hdl.handle.net/11336/199789
identifier_str_mv Echave, Julian; Wilke, Claus O.; Biophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence; Annual Reviews; Annual Review Of Biophysics; 46; 5-2017; 85-103
1936-122X
1936-1238
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.annualreviews.org/doi/10.1146/annurev-biophys-070816-033819
info:eu-repo/semantics/altIdentifier/doi/10.1146/annurev-biophys-070816-033819
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
dc.publisher.none.fl_str_mv Annual Reviews
publisher.none.fl_str_mv Annual Reviews
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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