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Biophys J, December 2000, p. 2987-3000, Vol. 79, No. 6
Institute for Medicine and Engineering, and School of Engineering and Applied Science, University of Pennsylvania, Philadelphia, Pennsylvania 19104 USA
The red cell's spectrin-actin network is known to
sustain local states of shear, dilation, and condensation, and yet the
short actin filaments are found to maintain membrane-tangent and
near-random azimuthal orientations. When calibrated with polarization
results for single actin filaments, imaging of micropipette-deformed
red cell ghosts has allowed an assessment of actin orientations and possible reorientations in the network. At the hemispherical cap of the
aspirated projection, where the network can be dilated severalfold,
filaments have the same membrane-tangent orientation as on a relatively
unstrained portion of membrane. Likewise, over the length of the
network projection pulled into the micropipette, where the network is
strongly sheared in axial extension and circumferential contraction,
actin maintains its tangent orientation and is only very weakly aligned
with network extension. Similar results are found for the integral
membrane protein Band 3. Allowing for thermal fluctuations, we deduce a
bound for the effective coupling constant,
, between network shear
and azimuthal orientation of the protofilament. The finding that
must be about an order of magnitude or more below its tight-coupling
value illustrates how nanostructural kinematics can decouple from more
macroscopic responses. Monte Carlo simulations of spectrin-actin
networks at ~10-nm resolution further support this conclusion and
substantiate an image of protofilaments as elements of a
high-temperature spin glass.
Biophys J, December 2000, p. 2987-3000, Vol. 79, No. 6
© 2000 by the Biophysical Society 0006-3495/00/12/2987/14 $2.00
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