A Hydrophobic Gating Mechanism for Nanopores
By O. Beckstein, Philip C. Biggin, M. Sansom. 2001
247 citations recorded by the source corpus.
Subfields: Biomedical Engineering, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/58bbe35327105aa4fc2c5648c284696afb49668b
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In Biomedical Engineering
In Molecular Biology
Citations in the corpus
- Water in nonpolar confinement: from nanotubes to proteins and beyond. (2008, unknown): “Drying and wetting of protein channels have been suggested as factors in channel gating (46, 136, 137).”
- Structure and gating mechanism of the acetylcholine receptor pore (2003, background): “The girdle therefore creates an energetic barrier to ion permeation across the lipid bilaye”
- Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map. (2005, background): “The density of atoms inside the pore fluctuates very little in time, indicating that the transmembrane pore of a-hemolysin is always filled with water, unlike the pore of MscS (Anishkin and Sukharev, 2004; Sotomayor and Schulten, 2004), or a generic hydrophobic nanopore of a similar radius (Beckstei”