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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/199789
Ver los metadatos del registro completo
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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 |
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Annual Reviews |
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CONICET Digital (CONICET) |
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Consejo Nacional de Investigaciones Científicas y Técnicas |
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CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
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dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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