Cargando…
Heterogeneous and rate-dependent streptavidin–biotin unbinding revealed by high-speed force spectroscopy and atomistic simulations
Receptor–ligand interactions are essential for biological function and their binding strength is commonly explained in terms of static lock-and-key models based on molecular complementarity. However, detailed information on the full unbinding pathway is often lacking due, in part, to the static natu...
Autores principales: | Rico, Felix, Russek, Andreas, González, Laura, Grubmüller, Helmut, Scheuring, Simon |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
National Academy of Sciences
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6452689/ https://www.ncbi.nlm.nih.gov/pubmed/30890636 http://dx.doi.org/10.1073/pnas.1816909116 |
Ejemplares similares
-
Streptavidin/biotin: Tethering geometry defines unbinding mechanics
por: Sedlak, Steffen M., et al.
Publicado: (2020) -
Host biotin is required for liver stage development in malaria parasites
por: Dellibovi-Ragheb, Teegan A., et al.
Publicado: (2018) -
Multiplexed protein force spectroscopy reveals equilibrium protein folding dynamics and the low-force response of von Willebrand factor
por: Löf, Achim, et al.
Publicado: (2019) -
Reconsideration of Dynamic Force Spectroscopy Analysis of Streptavidin-Biotin Interactions
por: Taninaka, Atsushi, et al.
Publicado: (2010) -
Awakening: Predicting external stimulation to force transitions between different brain states
por: Deco, Gustavo, et al.
Publicado: (2019)