AbstractTo understand the physics of polymer equilibrium and dynamics in the confines of ion channel pores, we study partitioning of poly(ethylene glycol)s (PEGs) of different molecular weights into the bacterial porin, OmpF. Thermodynamic and kinetic parameters of partitioning are deduced from the effects of polymer addition on ion currents through single OmpF channels reconstituted into planar lipid bilayer membranes. The equilibrium partition coefficient is inferred from the average reduction of channel conductance in the presence of PEG; rates of polymer exchange between the pore and the bulk are estimated from PEG-induced conductance noise. Partition coefficient as a function of polymer weight is best fitted by a “compressed exponentia...
The cell interior, enclosed by membrane barriers, is a condensed solution of inorganic ions, polymer...
We use two pore-forming proteins, alpha-hemolysin and aerolysin, to compare the polymer size-depende...
AbstractTo probe the size of the ion channel formed by Pseudomonas syringae lipodepsipeptide syringo...
AbstractTo understand the physics of polymer equilibrium and dynamics in the confines of ion channel...
ABSTRACT Polymer dynamics are of fundamental importance in materials science, biotechnology, and med...
Polymer dynamics are of fundamental importance in materials science, biotechnology, and medicine. Ho...
AbstractPolymer dynamics are of fundamental importance in materials science, biotechnology, and medi...
We study the interaction of neutral polyethylene glycol (PEG) molecules of different molecular weigh...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractPolymer dynamics are of fundamental importance in materials science, biotechnology, and medi...
AbstractThe trimeric OmpU and OmpT porins form large, triple-barrel hydrophilic channels in the oute...
AbstractUsing poly-(ethylene glycol)s of different molecular weights, we probe the channels formed i...
AbstractUsing poly-(ethylene glycol)s of different molecular weights, we probe the channels formed i...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractThe trimeric OmpU and OmpT porins form large, triple-barrel hydrophilic channels in the oute...
The cell interior, enclosed by membrane barriers, is a condensed solution of inorganic ions, polymer...
We use two pore-forming proteins, alpha-hemolysin and aerolysin, to compare the polymer size-depende...
AbstractTo probe the size of the ion channel formed by Pseudomonas syringae lipodepsipeptide syringo...
AbstractTo understand the physics of polymer equilibrium and dynamics in the confines of ion channel...
ABSTRACT Polymer dynamics are of fundamental importance in materials science, biotechnology, and med...
Polymer dynamics are of fundamental importance in materials science, biotechnology, and medicine. Ho...
AbstractPolymer dynamics are of fundamental importance in materials science, biotechnology, and medi...
We study the interaction of neutral polyethylene glycol (PEG) molecules of different molecular weigh...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractPolymer dynamics are of fundamental importance in materials science, biotechnology, and medi...
AbstractThe trimeric OmpU and OmpT porins form large, triple-barrel hydrophilic channels in the oute...
AbstractUsing poly-(ethylene glycol)s of different molecular weights, we probe the channels formed i...
AbstractUsing poly-(ethylene glycol)s of different molecular weights, we probe the channels formed i...
AbstractAsymmetrical (one-sided) application of penetrating water-soluble polymers, polyethylene gly...
AbstractThe trimeric OmpU and OmpT porins form large, triple-barrel hydrophilic channels in the oute...
The cell interior, enclosed by membrane barriers, is a condensed solution of inorganic ions, polymer...
We use two pore-forming proteins, alpha-hemolysin and aerolysin, to compare the polymer size-depende...
AbstractTo probe the size of the ion channel formed by Pseudomonas syringae lipodepsipeptide syringo...