A simple two-state protein unfolds mechanically via multiple heterogeneous pathways at single-molecule resolution
Previous investigations have indicated that the model protein CspB folds in a simple two-state fashion. Here, the authors provide direct experimental evidence for that the energy landscape of two-state folding proteins is highly heterogeneous and that unfolding can occur via multiple pathways.
Guardado en:
Autores principales: | Jörg Schönfelder, Raul Perez-Jimenez, Victor Muñoz |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2016
|
Materias: | |
Acceso en línea: | https://doaj.org/article/b0aaa035d8944396b1adbf1983ac4d33 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Quantifying accuracy and heterogeneity in single-molecule super-resolution microscopy
por: Hesam Mazidi, et al.
Publicado: (2020) -
Characterization of G-Quadruplexes Folding/Unfolding Dynamics and Interactions with Proteins from Single-Molecule Force Spectroscopy
por: Yuanlei Cheng, et al.
Publicado: (2021) -
On the physical mechanisms underlying single molecule dynamics in simple liquids
por: Russell G. Keanini, et al.
Publicado: (2021) -
Microfluidic deposition for resolving single-molecule protein architecture and heterogeneity
por: Francesco Simone Ruggeri, et al.
Publicado: (2018) -
Detecting structural heterogeneity in single-molecule localization microscopy data
por: Teun A.P.M. Huijben, et al.
Publicado: (2021)