Literature DB >> 64260

Influence of membrane thickness and ion concentration on the properties of the gramicidin a channel. Autocorrelation, spectral power density, relaxation and single-channel studies.

H A Kolb, E Bamberg.   

Abstract

The properties of the gramicidin A channel in membranes made from a series of monoglycerides have been studied. In agreement with previous studies, the dissociation rate constant kD of the dimeric channel was found to increase strongly with increasing chain length of the monoglyceride, corresponding to a decrease of the mean life-time of the channel. The value of kD, however, was not strictly correlated with the membrane thickness, as seen from a comparison of membranes with different solvent content. Furthermore, the life-time of the channel increased with the concentration of the permeable ion. This effect was tentatively explained by an electrostatic stabilization of the channel. The single-channel conductance lambda was found to decrease with increasing membrane thickness d, if d was varied by increasing the chain length of the lipid. On the other hand, if d was changed by varying the solvent content of the membranes formed from one and the same lipid, lambda remained constant. These observations were explained by the assumption of local inhomogeneities in the membrane thickness. A striking difference between the lambda values obtained from autocorrelation analysis in the presence of many presence of many channels (lambda a) and those obtained from single-channel experiments (lambda sc) occurred with membranes from longer chain-length monoglycerides. This difference disappeared at low ion concentrations. Electrostatic interactions between channels in local clusters were proposed for an interpretation of these findings.

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Year:  1977        PMID: 64260     DOI: 10.1016/0005-2736(77)90376-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  69 in total

1.  Covalently linked gramicidin channels: effects of linker hydrophobicity and alkaline metals on different stereoisomers.

Authors:  K M Armstrong; E P Quigley; P Quigley; D S Crumrine; S Cukierman
Journal:  Biophys J       Date:  2001-04       Impact factor: 4.033

2.  Statistical thermodynamics of membrane bending-mediated protein-protein attractions.

Authors:  T Chou; K S Kim; G Oster
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

3.  Membrane dipole potential modulates proton conductance through gramicidin channel: movement of negative ionic defects inside the channel.

Authors:  Tatyana I Rokitskaya; Elena A Kotova; Yuri N Antonenko
Journal:  Biophys J       Date:  2002-02       Impact factor: 4.033

4.  Voltage-dependent formation of gramicidin channels in lipid bilayers.

Authors:  J Sandblom; J Galvanovskis; B Jilderos
Journal:  Biophys J       Date:  2001-08       Impact factor: 4.033

5.  Gramicidin A channels switch between stretch activation and stretch inactivation depending on bilayer thickness.

Authors:  Boris Martinac; Owen P Hamill
Journal:  Proc Natl Acad Sci U S A       Date:  2002-03-19       Impact factor: 11.205

6.  Effects of permeant monovalent cations on end-plate channels.

Authors:  P W Gage; D Van Helden
Journal:  J Physiol       Date:  1979-03       Impact factor: 5.182

7.  A consistent model for thermal fluctuations and protein-induced deformations in lipid bilayers.

Authors:  Grace Brannigan; Frank L H Brown
Journal:  Biophys J       Date:  2005-12-02       Impact factor: 4.033

8.  Open channel noise. V. Fluctuating barriers to ion entry in gramicidin A channels.

Authors:  S H Heinemann; F J Sigworth
Journal:  Biophys J       Date:  1990-03       Impact factor: 4.033

9.  The permeation properties of small organic cations in gramicidin A channels.

Authors:  S A Seoh; D Busath
Journal:  Biophys J       Date:  1993-04       Impact factor: 4.033

10.  Characteristics of sodium and calcium conductance changes produced by membrane depolarization in an Aplysia neurone.

Authors:  D J Adams; P W Gage
Journal:  J Physiol       Date:  1979-04       Impact factor: 5.182

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