Defining the nature of thermal intermediate in 3 state folding proteins: apoflavodoxin, a study case.
The early stages of the thermal unfolding of apoflavodoxin have been determined by using atomistic multi microsecond-scale molecular dynamics (MD) simulations complemented with a variety of experimental techniques. Results strongly suggest that the intermediate is reached very early in the thermal u...
Guardado en:
Autores principales: | Rebeca García-Fandiño, Pau Bernadó, Sara Ayuso-Tejedor, Javier Sancho, Modesto Orozco |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Public Library of Science (PLoS)
2012
|
Materias: | |
Acceso en línea: | https://doaj.org/article/98e2b5b6f34847b29722140132b82605 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.
por: Simon Lindhoud, et al.
Publicado: (2012) -
Prediction and validation of protein intermediate states from structurally rich ensembles and coarse-grained simulations
por: Laura Orellana, et al.
Publicado: (2016) -
Pharmacological inactivation of the prion protein by targeting a folding intermediate
por: Giovanni Spagnolli, et al.
Publicado: (2021) -
Two energy barriers and a transient intermediate state determine the unfolding and folding dynamics of cold shock protein
por: Haiyan Hong, et al.
Publicado: (2021) -
CFTR trafficking mutations disrupt cotranslational protein folding by targeting biosynthetic intermediates
por: Hideki Shishido, et al.
Publicado: (2020)