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Biophys J, March 2001, p. 1075-1087, Vol. 80, No. 3
and
*Department of Biomathematics, UCLA School of Medicine, Los
Angeles, California 90095, USA,
Departments of Physiology
and Applied Mathematics and Theoretical Physics, University of
Cambridge, Cambridge CB3 9EW, United Kingdom, and
Department of Molecular and Cell Biology, University of
California, Berkeley, California 94720, USA
Highly wedge-shaped integral membrane proteins, or
membrane-adsorbed proteins can induce long-ranged deformations. The
strain in the surrounding bilayer creates relatively long-ranged forces that contribute to interactions with nearby proteins. In contrast, to
direct short-ranged interactions such as van der Waal's, hydrophobic, or electrostatic interactions, both local membrane Gaussian curvature and protein ellipticity can induce forces acting at distances of up to
a few times their typical radii. These forces can be attractive or
repulsive, depending on the proteins' shape, height, contact angle
with the bilayer, and a pre-existing local membrane curvature. Although
interaction energies are not pairwise additive, for sufficiently low
protein density, thermodynamic properties depend only upon pair
interactions. Here, we compute pair interaction potentials and entropic
contributions to the two-dimensional osmotic pressure of a collection
of noncircular proteins. For flat membranes, bending rigidities of
~100kBT, moderate ellipticities,
and large contact angle proteins, we find thermally averaged attractive interactions of order kBT. These
interactions may play an important role in the intermediate stages of
protein aggregation. Numerous biological processes where membrane
bending-mediated interactions may be relevant are cited, and possible
experiments are discussed.
Biophys J, March 2001, p. 1075-1087, Vol. 80, No. 3
© 2001 by the Biophysical Society 0006-3495/01/03/1075/13 $2.00
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