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Biophys J, January 1999, p. 314-322, Vol. 76, No. 1
*Department of Pathology, University of Alabama, Birmingham, Birmingham, Alabama 35294; #Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110; and §Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27110 USA
Proteins in plasma membranes diffuse more slowly than
proteins inserted into artificial lipid bilayers. On a long-range scale (>250 nm), submembrane barriers, or skeleton fences that hinder long-range diffusion and create confinement zones, have been described. Even within such confinement zones, however, diffusion of proteins is
much slower than predicted by the viscosity of the lipid. The cause of
this slowing of diffusion on the micro scale has not been determined
and is the focus of this paper. One way to approach this question is to
determine the dependence of particle motion on particle size. Some
current models predict that the diffusion coefficient of a membrane
protein aggregate will depend strongly on its size, while others do
not. We have measured the diffusion coefficients of membrane
glycoprotein aggregates linked together by concanavalin A molecules
bound to beads of various sizes, and also the diffusion coefficients of
individual concanavalin A binding proteins. The measurements
demonstrate at most a weak dependence of diffusion coefficient on
aggregate size. This finding supports retardation by viscous effects,
and is not consistent with models involving direct interaction of
diffusing proteins with cytoskeletal elements.
Biophys J, January 1999, p. 314-322, Vol. 76, No. 1
© 1999 by the Biophysical Society 0006-3495/99/01/314/09 $2.00
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