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dc.contributor.author
Echave, Julián
dc.contributor.author
Jackson, Eleisha L.
dc.contributor.author
Wilke, Claus O.
dc.date.available
2018-03-09T15:37:56Z
dc.date.issued
2015-04
dc.identifier.citation
Echave, Julián; Jackson, Eleisha L.; Wilke, Claus O.; Relationship between protein thermodynamic constraints and variation of evolutionary rates among sites; IOP Publishing; Physical Biology; 12; 2; 4-2015; 1-8
dc.identifier.issn
1478-3967
dc.identifier.uri
http://hdl.handle.net/11336/38399
dc.description.abstract
Evolutionary-rate variation among sites within proteins depends on functional and biophysical properties that constrain protein evolution. It is generally accepted that proteins must be able to fold stably in order to function. However, the relationship between stability constraints and among-sites rate variation is not well understood. Here, we present a biophysical model that links the thermodynamic stability changes due to mutations at sites in proteins (ΔΔG) to the rate at which mutations accumulate at those sites over evolutionary time. We find that such a 'stability model' generally performs well, displaying correlations between predicted and empirically observed rates of up to 0.75 for some proteins. We further find that our model has comparable predictive power as does an alternative, recently proposed 'stress model' that explains evolutionary-rate variation among sites in terms of the excess energy needed for mutants to adopt the correct active structure (ΔΔG∗). The two models make distinct predictions, though, and for some proteins the stability model outperforms the stress model and vice versa. We conclude that both stability and stress constrain site-specific sequence evolution in proteins.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
IOP Publishing
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
Biophysical Model
dc.subject
Protein Evolution
dc.subject
Rate Variation Among Sites
dc.subject
Stability
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Stress
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Thermodynamics
dc.subject.classification
Otras Ciencias Químicas
dc.subject.classification
Ciencias Químicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Relationship between protein thermodynamic constraints and variation of evolutionary rates among sites
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-08T18:59:46Z
dc.journal.volume
12
dc.journal.number
2
dc.journal.pagination
1-8
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Echave, Julián. Universidad Nacional de San Martín. Escuela de Ciencia y Tecnología; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Jackson, Eleisha L.. University of Texas at Austin; Estados Unidos
dc.description.fil
Fil: Wilke, Claus O.. University of Texas at Austin; Estados Unidos
dc.journal.title
Physical Biology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1088/1478-3975/12/2/025002
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://iopscience.iop.org/article/10.1088/1478-3975/12/2/025002
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4391963/
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