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Journal of Bioloscel Physics OO: 1-28, 2003. 1 18.2003 Aluwer Academic Publishers. Printed inthe Netherlands Models of the Collective Behavior of Proteins in Cells: Tubulin, Actin and Motor Proteins JA. TUSZYNSKT and J.A. BROWN Department of Physics, Universiy ofAlbere, Edmonton, Albena, T6G 211, Canada “also ote Laboratory of Bimolecular Dynamics, Catholic University of Lewven, Celesiinenaan 2000, B-3001, Belgium D. SEPT. Department of Biomedicad Engineering, Center for Computational Biology. Washington University, Campus Box 1087, One Brookings Drive St. Louis, MO 63130-4898, USA Abstract, One of the most important issues of molecular biophysics is the complex and mult Functional behavior ofthe cell's eytesheleton. Interiors of living cells are sructurlly organized by the cytoskeleton networks of filamentous protein polymers: microtubules, actin and intermediate filaments with motor proteins providing force and directionality needed for transport processes. “Microtubules (M's) take active parti material tansport within the cell, constitute the most rigid clement ofthe cell and henoe foond many uses in cell motility (eg, lagella and cis). At present there is, however, no quanttvelypeediciable explanation of how these important phenomena are orchestrated at a molecular level Moreover, microtubules have been demonsuated to selF-organize Jeading to patern formation, We discuss here several models which attempt to shed light on the assembly of microtubules and their interactions with motor proves. Subsequently, an overview of ‘sctn filaments and thir properties is given with particlac emphasis on actin assembly processes. ‘The lengths of set filaments have been reported that were foie by spontaneous polymerization of highly purified atin monomers after Ibeling with todamine-phalfldts. Te length tisrbutions fre exponential with a nian of about 7 jan. This lengih iy independent of tbe inital cancentra- tion of actin monomer, an observation inconsistent with 2 sirmpe nuclestion-

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