| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Biophys J, January 1999, p. 129-148, Vol. 76, No. 1
*Istituto Nazionale per la Fisica della Materia,
This paper shows that the selectivity properties of
monovalent cation channels found in biological membranes can originate simply from geometrical properties of the inner core of the channel without any critical contribution from electrostatic interactions between the permeating ions and charged or polar groups. By using well-known techniques of statistical mechanics, such as the Langevin equations and Kramer theory of reaction rates, a theoretical equation is provided relating the permeability ratio
PB/PA between ions A and
B to simple physical properties, such as channel geometry, thermodynamics of ion hydration, and electrostatic interactions between
the ion and charged (or polar) groups. Diffusive corrections and
recrossing rates are also considered and evaluated. It is shown that
the selectivity found in usual K+, gramicidin,
Na+, cyclic nucleotide gated, and end plate channels can be
explained also in the absence of any charged or polar group.
If these groups are present, they significantly change the permeability
ratio only if the ion at the selectivity filter is in van der Waals contact with them, otherwise these groups simply affect the channel conductance, lowering the free energy barrier of the same amount for
the two ions, thus explaining why single channel conductance, as it is
experimentally observed, can be very different in channels sharing the
same selectivity sequence. The proposed theory also provides an
estimate of channel minimum radius for K+, gramicidin,
Na+, and cyclic nucleotide gated channels.
Biophys J, January 1999, p. 129-148, Vol. 76, No. 1
© 1999 by the Biophysical Society 0006-3495/99/01/129/20 $2.00
This article has been cited by other articles:
![]() |
G. V. Miloshevsky and P. C. Jordan Conformational Changes in the Selectivity Filter of the Open-State KcsA Channel: An Energy Minimization Study Biophys. J., October 1, 2008; 95(7): 3239 - 3251. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Giorgetti, P. Carloni, P. Mistrik, and V. Torre A Homology Model of the Pore Region of HCN Channels Biophys. J., August 1, 2005; 89(2): 932 - 944. [Abstract] [Full Text] [PDF] |
||||
![]() |
B. M. Schmitt and H. Koepsell Alkali Cation Binding and Permeation in the Rat Organic Cation Transporter rOCT2 J. Biol. Chem., July 1, 2005; 280(26): 24481 - 24490. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. Cohen and K. Schulten Mechanism of Anionic Conduction across ClC Biophys. J., February 1, 2004; 86(2): 836 - 845. [Abstract] [Full Text] [PDF] |
||||
![]() |
P. Roncaglia, P. Mistrik, and V. Torre Pore Topology of the Hyperpolarization-Activated Cyclic Nucleotide-Gated Channel from Sea Urchin Sperm Biophys. J., October 1, 2002; 83(4): 1953 - 1964. [Abstract] [Full Text] [PDF] |
||||
![]() |
S. C. Hinnah, R. Wagner, N. Sveshnikova, R. Harrer, and J. Soll The Chloroplast Protein Import Channel Toc75: Pore Properties and Interaction with Transit Peptides Biophys. J., August 1, 2002; 83(2): 899 - 911. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |