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dc.contributor.author
Vila, Jorge Alberto
dc.date.available
2024-02-19T11:54:06Z
dc.date.issued
2023-08
dc.identifier.citation
Vila, Jorge Alberto; Protein folding rate evolution upon mutations; Springer; Biophysical Reviews; 15; 4; 8-2023; 661-669
dc.identifier.issn
1867-2450
dc.identifier.uri
http://hdl.handle.net/11336/227373
dc.description.abstract
Despite the spectacular success of cutting-edge protein fold prediction methods, many critical questions remain unanswered, including why proteins can reach their native state in a biologically reasonable time. A satisfactory answer to this simple question could shed light on the slowest folding rate of proteins as well as how mutations—amino-acid substitutions and/or post-translational modifications—might affect it. Preliminary results indicate that (i) Anfinsen’s dogma validity ensures that proteins reach their native state on a reasonable timescale regardless of their sequence or length, and (ii) it is feasible to determine the evolution of protein folding rates without accounting for epistasis effects or the mutational trajectories between the starting and target sequences. These results have direct implications for evolutionary biology because they lay the groundwork for a better understanding of why, and to what extent, mutations—a crucial element of evolution and a factor influencing it—affect protein evolvability. Furthermore, they may spur significant progress in our efforts to solve crucial structural biology problems, such as how a sequence encodes its folding.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
ANFINSEN DOGMA
dc.subject
EVOLUTION
dc.subject
FOLDING RATE
dc.subject
LEVINTHAL PARADOX
dc.subject
MUTATIONS
dc.subject
POST-TRANSLATIONAL MODIFICATIONS
dc.subject
PROTEIN MARGINAL STABILITY
dc.subject.classification
Física Atómica, Molecular y Química
dc.subject.classification
Ciencias Físicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Protein folding rate evolution upon mutations
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-02-19T10:22:40Z
dc.identifier.eissn
1867-2469
dc.journal.volume
15
dc.journal.number
4
dc.journal.pagination
661-669
dc.journal.pais
Alemania
dc.journal.ciudad
Berlín
dc.description.fil
Fil: Vila, Jorge Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - San Luis. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi". Universidad Nacional de San Luis. Facultad de Ciencias Físico, Matemáticas y Naturales. Instituto de Matemática Aplicada de San Luis "Prof. Ezio Marchi"; Argentina
dc.journal.title
Biophysical Reviews
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s12551-023-01088-z
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s12551-023-01088-z
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