Cargando…
Making Monomeric Aquaporin Z by Disrupting the Hydrophobic Tetramer Interface
[Image: see text] The assembly of integral membrane proteins depends on the packing of hydrophobic interfaces. The forces driving this packing remain unclear. In this study, we have investigated the effect of mutations in these hydrophobic interfaces on the structure and function of the tetrameric E...
Autores principales: | Schmidt, Victoria, Sturgis, James N. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2017
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6641176/ https://www.ncbi.nlm.nih.gov/pubmed/31457635 http://dx.doi.org/10.1021/acsomega.7b00261 |
Ejemplares similares
-
Zinc Modulation of Water Permeability Reveals that Aquaporin 0 Functions as a Cooperative Tetramer
por: Németh-Cahalan, Karin L., et al.
Publicado: (2007) -
The Subcellular Localization of an Aquaporin-2 Tetramer Depends on the Stoichiometry of Phosphorylated and Nonphosphorylated Monomers
por: Kamsteeg, E.J., et al.
Publicado: (2000) -
Nucleosome accessibility governed by the dimer/tetramer interface
por: Böhm, Vera, et al.
Publicado: (2011) -
Perturbation of the Monomer–Monomer
Interfaces
of the Benzoylformate Decarboxylase Tetramer
por: Andrews, Forest H., et al.
Publicado: (2014) -
Biophysical Characterization of the Dimer and Tetramer Interface Interactions of the Human Cytosolic Malic Enzyme
por: Murugan, Sujithkumar, et al.
Publicado: (2012)