Cargando…
Divergent evolution of protein conformational dynamics in dihydrofolate reductase
Molecular evolution is driven by mutations, which may affect the fitness of an organism and are then subject to natural selection or genetic drift. Analysis of primary protein sequences and tertiary structures has yielded valuable insights into the evolution of protein function, but little is known...
Autores principales: | Bhabha, Gira, Ekiert, Damian C., Jennewein, Madeleine, Zmasek, Christian M., Tuttle, Lisa M., Kroon, Gerard, Dyson, H. Jane, Godzik, Adam, Wilson, Ian A., Wright, Peter E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3823643/ https://www.ncbi.nlm.nih.gov/pubmed/24077226 http://dx.doi.org/10.1038/nsmb.2676 |
Ejemplares similares
-
Side Chain Conformational Averaging in Human Dihydrofolate
Reductase
por: Tuttle, Lisa M., et al.
Publicado: (2014) -
Cofactor-Mediated
Conformational Dynamics Promote
Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway
por: Oyen, David, et al.
Publicado: (2015) -
Minimization of dynamic effects in the evolution of dihydrofolate reductase
por: Ruiz-Pernía, J. Javier, et al.
Publicado: (2016) -
Tales of Dihydrofolate Binding to R67 Dihydrofolate
Reductase
por: Duff, Michael R., et al.
Publicado: (2015) -
Evolution
Alters the Enzymatic Reaction
Coordinate of Dihydrofolate
Reductase
por: Masterson, Jean E., et al.
Publicado: (2014)