Cargando…
Thermodynamic and Evolutionary Coupling between the Native and Amyloid State of Globular Proteins
The amyloid-like aggregation propensity present in most globular proteins is generally considered to be a secondary side effect resulting from the requirements of protein stability. Here, we demonstrate, however, that mutations in the globular and amyloid state are thermodynamically correlated rathe...
Autores principales: | Langenberg, Tobias, Gallardo, Rodrigo, van der Kant, Rob, Louros, Nikolaos, Michiels, Emiel, Duran-Romaña, Ramon, Houben, Bert, Cassio, Rafaela, Wilkinson, Hannah, Garcia, Teresa, Ulens, Chris, Van Durme, Joost, Rousseau, Frederic, Schymkowitz, Joost |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7175379/ https://www.ncbi.nlm.nih.gov/pubmed/32294448 http://dx.doi.org/10.1016/j.celrep.2020.03.076 |
Ejemplares similares
-
Structural hot spots for the solubility of globular proteins
por: Ganesan, Ashok, et al.
Publicado: (2016) -
Accurate Prediction of DnaK-Peptide Binding via Homology Modelling and Experimental Data
por: Van Durme, Joost, et al.
Publicado: (2009) -
Exploiting the aggregation propensity of beta-lactamases to design inhibitors that induce enzyme misfolding
por: Khodaparast, Ladan, et al.
Publicado: (2023) -
Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments
por: Michiels, Emiel, et al.
Publicado: (2020) -
Mechanisms and therapeutic potential of interactions between human amyloids and viruses
por: Michiels, Emiel, et al.
Publicado: (2020)