Cargando…
From Microstates to Macrostates in the Conformational Dynamics of GroEL: A Single-Molecule Förster Resonance Energy Transfer Study
[Image: see text] The chaperonin GroEL is a multisubunit molecular machine that assists in protein folding in the Escherichia coli cytosol. Past studies have shown that GroEL undergoes large allosteric conformational changes during its reaction cycle. Here, we report single-molecule Förster resonanc...
Autores principales: | Liebermann, Demian G., Jungwirth, Jakub, Riven, Inbal, Barak, Yoav, Levy, Dorit, Horovitz, Amnon, Haran, Gilad |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10388350/ https://www.ncbi.nlm.nih.gov/pubmed/37440608 http://dx.doi.org/10.1021/acs.jpclett.3c01281 |
Ejemplares similares
-
Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
por: Korobko, Ilia, et al.
Publicado: (2020) -
Slowdown of Water Dynamics from the Top to the Bottom
of the GroEL Cavity
por: Macro, Nicolas, et al.
Publicado: (2021) -
Probing
Water Density and Dynamics in the Chaperonin GroEL Cavity
por: Franck, John M., et al.
Publicado: (2014) -
A diminished hydrophobic effect inside the GroEL/ES cavity contributes to protein substrate destabilization
por: Korobko, Ilia, et al.
Publicado: (2022) -
Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL
por: Moparthi, Satish Babu, et al.
Publicado: (2013)