Cargando…
Multiple Routes and Milestones in the Folding of HIV–1 Protease Monomer
Proteins fold on a time scale incompatible with a mechanism of random search in conformational space thus indicating that somehow they are guided to the native state through a funneled energetic landscape. At the same time the heterogeneous kinetics suggests the existence of several different foldin...
Autores principales: | Bonomi, Massimiliano, Barducci, Alessandro, Gervasio, Francesco L., Parrinello, Michele |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2954147/ https://www.ncbi.nlm.nih.gov/pubmed/20967249 http://dx.doi.org/10.1371/journal.pone.0013208 |
Ejemplares similares
-
Insight into the Folding Inhibition of the HIV-1 Protease by a Small Peptide
por: Bonomi, Massimiliano, et al.
Publicado: (2007) -
High-resolution structure of a retroviral protease folded as a monomer
por: Gilski, Miroslaw, et al.
Publicado: (2011) -
The evolution of the HIV-1 protease folding stability
por: Ferreiro, David, et al.
Publicado: (2022) -
Polymers without
Petrochemicals: Sustainable Routes
to Conventional Monomers
por: Hayes, Graham, et al.
Publicado: (2022) -
Handcuffing reversal is facilitated by proteases and replication initiator monomers
por: Bury, Katarzyna, et al.
Publicado: (2017)