AbstractThe aquaglyceroporin GlpF is a transmembrane channel of Escherichia coli that facilitates the uptake of glycerol by the cell. Its high glycerol uptake rate is crucial for the cell to survive in very low glycerol concentrations. Although GlpF allows both influx and outflux of glycerol, its structure, similar to the structure of maltoporin, exhibits a significant degree of asymmetry. The potential of mean force characterizing glycerol in the channel shows a corresponding asymmetry with an attractive vestibule only at the periplasmic side. In this study, we analyze the potential of mean force, showing that a simplified six-step model captures the kinetics and yields a glycerol conduction rate that agrees well with observation. The vest...
The structures of several aquaglyceroporins have been resolved to atomic resolution showing two or m...
AbstractThe structure of a glycerol channel from Escherichia coli at 2.2 Å resolution serves as a ba...
Water and glycerol permeation via human AQP3 are described exploiting advanced metadynamics approach...
AbstractThe aquaglyceroporin GlpF is a transmembrane channel of Escherichia coli that facilitates th...
AbstractThe glycerol uptake facilitator, GlpF, a major intrinsic protein found in Escherichia coli, ...
AbstractAmong aquaglyceroporins that transport both water and glycerol across the cell membrane, Esc...
AbstractBackground: The E. coli glycerol facilitator, GlpF, selectively conducts glycerol and water,...
SummaryThe recent availability of high-resolution structures of two structurally highly homologous, ...
The aqua (glycero) porins conduct water (and glycerol) across cell membranes. The structure of these...
URL:http://link.aps.org/doi/10.1103/PhysRevLett.93.238102 DOI:10.1103/PhysRevLett.93.238102Channel ...
AbstractWater permeation and electrostatic interactions between water and channel are investigated i...
A large family of membrane channel proteins selective for transport of water (aquaporins) or water p...
AbstractThe aquaglyceroporins of Escherichia coli, EcGlpF, and of Plasmodium falciparum, PfAQP, are ...
The three-dimensional structure of GlpF, the glycerol facilitator of Escherichia coli, was determine...
The three-dimensional structure of GlpF, the glycerol facilitator of Escherichia coli, was determine...
The structures of several aquaglyceroporins have been resolved to atomic resolution showing two or m...
AbstractThe structure of a glycerol channel from Escherichia coli at 2.2 Å resolution serves as a ba...
Water and glycerol permeation via human AQP3 are described exploiting advanced metadynamics approach...
AbstractThe aquaglyceroporin GlpF is a transmembrane channel of Escherichia coli that facilitates th...
AbstractThe glycerol uptake facilitator, GlpF, a major intrinsic protein found in Escherichia coli, ...
AbstractAmong aquaglyceroporins that transport both water and glycerol across the cell membrane, Esc...
AbstractBackground: The E. coli glycerol facilitator, GlpF, selectively conducts glycerol and water,...
SummaryThe recent availability of high-resolution structures of two structurally highly homologous, ...
The aqua (glycero) porins conduct water (and glycerol) across cell membranes. The structure of these...
URL:http://link.aps.org/doi/10.1103/PhysRevLett.93.238102 DOI:10.1103/PhysRevLett.93.238102Channel ...
AbstractWater permeation and electrostatic interactions between water and channel are investigated i...
A large family of membrane channel proteins selective for transport of water (aquaporins) or water p...
AbstractThe aquaglyceroporins of Escherichia coli, EcGlpF, and of Plasmodium falciparum, PfAQP, are ...
The three-dimensional structure of GlpF, the glycerol facilitator of Escherichia coli, was determine...
The three-dimensional structure of GlpF, the glycerol facilitator of Escherichia coli, was determine...
The structures of several aquaglyceroporins have been resolved to atomic resolution showing two or m...
AbstractThe structure of a glycerol channel from Escherichia coli at 2.2 Å resolution serves as a ba...
Water and glycerol permeation via human AQP3 are described exploiting advanced metadynamics approach...