Cargando…
Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study
[Image: see text] The folding of proteins into their native conformation is a complex process that has been extensively studied over the past half-century. The ribosome, the molecular machine responsible for protein synthesis, is known to interact with nascent proteins, adding further complexity to...
Autores principales: | Vu, Quyen V., Nissley, Daniel A., Jiang, Yang, O’Brien, Edward P., Li, Mai Suan |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2023
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10240488/ https://www.ncbi.nlm.nih.gov/pubmed/37200608 http://dx.doi.org/10.1021/acs.jpcb.3c01694 |
Ejemplares similares
-
The driving force for co-translational protein folding is weaker in the ribosome vestibule due to greater water ordering
por: Vu, Quyen V., et al.
Publicado: (2021) -
Cocktail of REGN Antibodies Binds More Strongly to
SARS-CoV-2 Than Its Components, but the Omicron Variant Reduces
Its Neutralizing Ability
por: Nguyen, Hung, et al.
Publicado: (2022) -
Kinetic and structural comparison of a protein’s cotranslational folding and refolding pathways
por: Samelson, Avi J., et al.
Publicado: (2018) -
Does SARS-CoV-2 Bind to Human ACE2 More Strongly
Than Does SARS-CoV?
por: Nguyen, Hoang Linh, et al.
Publicado: (2020) -
Electrostatic Interactions Explain the Higher Binding
Affinity of the CR3022 Antibody
for SARS-CoV-2 than the 4A8 Antibody
por: Nguyen, Hung, et al.
Publicado: (2021)