Channel access resistance has been measured to estimate the characteristic size of a single ion channel. We compare channel conductance in the presence of nonpenetrating water-soluble polymers with that obtained for polymer-free electrolyte solution. The contribution of the access resistance to the total alamethicin channel resistance is approximately 10% for first three open channel levels. The open alamethicin channel radii inferred for these first three levels from the access resistance are 6.3, 10.3, and 11.4 A. The dependence of channel conductance on polymer molecular weight also allows evaluation of the channel dimensions from polymer exclusion. Despite varying conductance, it was shown that steric radii of the alamethicin channel at...
AbstractPartitioning of ethylene glycol and its polymeric forms into the pore of the volume-sensitiv...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting ...
Channel access resistance has been measured to estimate the characteristic size of a single ion chan...
Contrary to expectations based on heightened solution viscosity, alamethicin channels appear to spee...
Molecular structures of transmembrane channels formed by alamethicin polypeptide aggregates were ana...
AbstractTo probe the volume changes of the voltage-dependent anion-selective channel (VDAC), the non...
Covalent dimers of alamethicin form conducting structures with gating properties that permit measure...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractTo understand the physics of polymer equilibrium and dynamics in the confines of ion channel...
The ion currents induced by alamethicin were investigated in unilamellar vesicles using electron par...
Alamethicin, a 20-amino acid peptide, has been studied for a number of years as a model for voltage-...
Synthetic nanopores and mesoscopic protein channels have common traits like the importance of electr...
Single-channel conductance measurements in biological pores have demonstrated the importance of inte...
Conductance noise measurement of the open states of alamethicin transmembrane channels reveals exces...
AbstractPartitioning of ethylene glycol and its polymeric forms into the pore of the volume-sensitiv...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting ...
Channel access resistance has been measured to estimate the characteristic size of a single ion chan...
Contrary to expectations based on heightened solution viscosity, alamethicin channels appear to spee...
Molecular structures of transmembrane channels formed by alamethicin polypeptide aggregates were ana...
AbstractTo probe the volume changes of the voltage-dependent anion-selective channel (VDAC), the non...
Covalent dimers of alamethicin form conducting structures with gating properties that permit measure...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractTo understand the physics of polymer equilibrium and dynamics in the confines of ion channel...
The ion currents induced by alamethicin were investigated in unilamellar vesicles using electron par...
Alamethicin, a 20-amino acid peptide, has been studied for a number of years as a model for voltage-...
Synthetic nanopores and mesoscopic protein channels have common traits like the importance of electr...
Single-channel conductance measurements in biological pores have demonstrated the importance of inte...
Conductance noise measurement of the open states of alamethicin transmembrane channels reveals exces...
AbstractPartitioning of ethylene glycol and its polymeric forms into the pore of the volume-sensitiv...
Alamethicin and its analogs from cation selective, multi-conductance channels in lipid bilayers. The...
Aquaporins are membrane channels selectively permeated by water or water plus glycerol. Conflicting ...