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Biophys J, March 2002, p. 1329-1337, Vol. 82, No. 3
Department of Physiology, Loyola University Medical School, Maywood, Illinois 60153 USA
The submillisecond closing events (flickers) and the
single channel conductances to protons (gH)
were studied in native gramicidin A (gA) and in the SS and
RR diastereoisomers of dioxolane-linked gA channels in planar
bilayers. Bilayers were formed from glycerylmonooleate (GMO) in various
solvents. In GMO/decane (thick) bilayers, the largest flicker frequency
occurred in the SS channel (39 s
1), followed by the RR (4 s
1) and native gA channels (3 s
1). These
frequencies were attenuated in GMO/squalene (thin) bilayers by 100-, 30-, and 70-fold in the SS, RR, and native gA channels, respectively.
In thin bilayers, the average burst duration of native gA channels was
30-fold longer than in thick bilayers. The RR dioxolane-linked gA dimer
"inactivated" in GMO/decane but not in squalene-containing
bilayers. The mean closed time of flickers (~0.12 ms) was essentially
the same in various gA channels. In thin bilayers,
gH values were larger by ~10% (SS), 30%
(RR), and 20% (native gA) in relation to thick bilayers. It is
concluded that flickers are not related to pre-dissociation or
dissociation states of gA monomers, and do not seem to be caused by
intrinsic conformational changes of channel proteins. It is proposed
that flickers are caused by undulations of the bilayer that obliterate the openings of gA channels. Differences between flicker frequencies in
various gA channels are likely to result from variations in channel
geometries at the bilayer/channel interface. The smaller gH in thick bilayers suggests that the
deformation of these bilayers around the gA channel creates a
diffusional pathway next to the mouths of the channel that is longer
and more restrictive than in thin GMO bilayers. A possible molecular
interpretation for these effects is attempted.
Biophys J, March 2002, p. 1329-1337, Vol. 82, No. 3
© 2002 by the Biophysical Society 0006-3495/02/03/1329/09 $2.00
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