Facilitated substrate transport through membrane proteins. Academic Article

abstract

• Substrate transport through the membrane protein maltoporin is facilitated by an affinity site in the channel. The analysis of the ion current fluctuations induced by penetration of the sugar into the channel yields the kinetic constants. Modification of the affinity site by replacing the aromatic residues suggests that nature has optimized the channel protein for maximum affinity at the extracellular side, as well as for an increased off-rate to eject a sugar trapped in the pore towards the periplasmic side.

authors

• Hilty, Christian

published proceedings

• Phys Rev Lett

author list (cited authors)

• Hilty, C., & Winterhalter, M.

citation count

• 40

complete list of authors

• Hilty, C||Winterhalter, M

publication date

• June 2001

publisher

• American Physical Society (APS)  Publisher

published in

• Physical Review Letters  Journal

keywords

• Bacterial Outer Membrane Proteins
• Biological Transport
• Kinetics
• Lipid Bilayers
• Membrane Potentials
• Membrane Proteins
• Mutagenesis
• Oligosaccharides
• Porins
• Receptors, Virus
• Thermodynamics
• Trisaccharides

PubMed Central ID

• 11415317

Digital Object Identifier (DOI)

• 10.1103/PhysRevLett.86.5624

start page

• 5624

end page

• 5627

volume

• 86

issue

• 24

URL

• http%3A%2F%2Fdx.doi.org%2F10.1103%2Fphysrevlett.86.5624