Cargando…
Order through Disorder: Hyper-Mobile C-Terminal Residues Stabilize the Folded State of a Helical Peptide. A Molecular Dynamics Study
Conventional wisdom has it that the presence of disordered regions in the three-dimensional structures of polypeptides not only does not contribute significantly to the thermodynamic stability of their folded state, but, on the contrary, that the presence of disorder leads to a decrease of the corre...
Autores principales: | Patapati, Kalliopi K., Glykos, Nicholas M. |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2010
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3004869/ https://www.ncbi.nlm.nih.gov/pubmed/21187962 http://dx.doi.org/10.1371/journal.pone.0015290 |
Ejemplares similares
-
Folding Molecular Dynamics Simulation of a gp41-Derived
Peptide Reconcile Divergent Structure Determinations
por: Georgoulia, Panagiota S., et al.
Publicado: (2018) -
To Fold or
Not to Fold: Diastereomeric Optimization
of an α-Helical Antimicrobial Peptide
por: Personne, Hippolyte, et al.
Publicado: (2023) -
Systematic Design and Validation of Ion Channel Stabilization
of Amphipathic α-Helical Peptides Incorporating Tryptophan
Residues
por: Shigedomi, Keita, et al.
Publicado: (2020) -
Folding and Insertion of Transmembrane Helices at the ER
por: Whitley, Paul, et al.
Publicado: (2021) -
The properties conferred upon triple-helical collagen-mimetic peptides by the presence of cysteine residues
por: Slatter, David A., et al.
Publicado: (2012)