Cargando…
Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
Intrinsically disordered linkers provide multi-domain proteins with degrees of conformational freedom that are often essential for function. These highly dynamic assemblies represent a significant fraction of all proteomes, and deciphering the physical basis of their interactions represents a consid...
Autores principales: | Delaforge, Elise, Milles, Sigrid, Huang, Jie-rong, Bouvier, Denis, Jensen, Malene Ringkjøbing, Sattler, Michael, Hart, Darren J., Blackledge, Martin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5020063/ https://www.ncbi.nlm.nih.gov/pubmed/27679800 http://dx.doi.org/10.3389/fmolb.2016.00054 |
Ejemplares similares
-
Binding Mechanisms of Intrinsically Disordered Proteins: Theory, Simulation, and Experiment
por: Mollica, Luca, et al.
Publicado: (2016) -
Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
por: Camacho-Zarco, Aldo R., et al.
Publicado: (2020) -
Enthalpy–Entropy Compensation in the Promiscuous Interaction of an Intrinsically Disordered Protein with Homologous Protein Partners
por: Kragelj, Jaka, et al.
Publicado: (2021) -
Quantitative
Description of Intrinsically Disordered
Proteins Using Single-Molecule FRET, NMR, and SAXS
por: Naudi-Fabra, Samuel, et al.
Publicado: (2021) -
Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains
por: Dempsey, Christopher E., et al.
Publicado: (2019)