Protein flexibility facilitates quaternary structure assembly and evolution.
The intrinsic flexibility of proteins allows them to undergo large conformational fluctuations in solution or upon interaction with other molecules. Proteins also commonly assemble into complexes with diverse quaternary structure arrangements. Here we investigate how the flexibility of individual pr...
Guardado en:
Autores principales: | Joseph A Marsh, Sarah A Teichmann |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2014
|
Materias: | |
Acceso en línea: | https://doaj.org/article/3cc2f684f89048daa8ed385d071c5551 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Cohesive versus flexible evolution of functional modules in eukaryotes.
por: Like Fokkens, et al.
Publicado: (2009) -
Structure and age jointly influence rates of protein evolution.
por: Macarena Toll-Riera, et al.
Publicado: (2012) -
Exploring the evolution of novel enzyme functions within structurally defined protein superfamilies.
por: Nicholas Furnham, et al.
Publicado: (2012) -
Fusion of protein aggregates facilitates asymmetric damage segregation.
por: Miguel Coelho, et al.
Publicado: (2014) -
Quaternary structure of pathological prion protein as a determining factor of strain-specific prion replication dynamics.
por: Florent Laferrière, et al.
Publicado: (2013)