Cargando…
The Effects of Sodium Ions on Ligand Binding and Conformational States of G Protein-Coupled Receptors—Insights from Mass Spectrometry
[Image: see text] The use of mass spectrometry to investigate proteins is now well established and provides invaluable information for both soluble and membrane protein assemblies. Maintaining transient noncovalent interactions under physiological conditions, however, remains challenging. Here, usin...
Autores principales: | Agasid, Mark T., Sørensen, Lars, Urner, Leonhard H., Yan, Jun, Robinson, Carol V. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2021
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7995251/ https://www.ncbi.nlm.nih.gov/pubmed/33711230 http://dx.doi.org/10.1021/jacs.0c11837 |
Ejemplares similares
-
Emergence of mass spectrometry detergents for membrane proteomics
por: Behnke, Jan-Simon, et al.
Publicado: (2023) -
Ligand binding to a G protein–coupled receptor captured in a mass spectrometer
por: Yen, Hsin-Yung, et al.
Publicado: (2017) -
Exploring the Potential of Dendritic Oligoglycerol Detergents for Protein Mass Spectrometry
por: Urner, Leonhard H., et al.
Publicado: (2018) -
Nanoscale Ion Emitters in Native Mass Spectrometry
for Measuring Ligand–Protein Binding Affinities
por: Nguyen, Giang T. H., et al.
Publicado: (2019) -
Conformational Dynamics of DNA G-Quadruplex in Solution Studied by Kinetic Capillary Electrophoresis Coupled On-line with Mass Spectrometry
por: Berezovski, Maxim V
Publicado: (2014)