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Atomistic simulation of protein evolution reveals sequence covariation and time-dependent fluctuations of site-specific substitution rates

Thermodynamic stability is a crucial fitness constraint in protein evolution and is a central factor in shaping the sequence landscapes of proteins. The correlation between stability and molecular fitness depends on the mechanism that relates the biophysical property with biological function. In the...

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Detalles Bibliográficos
Autores principales: Norn, Christoffer, André, Ingemar
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10075473/
https://www.ncbi.nlm.nih.gov/pubmed/36961827
http://dx.doi.org/10.1371/journal.pcbi.1010262