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Osmotic Pressure: A Tool to Investigate the Polymeric Forms of Actin pp. 97-136 $100.00
Authors:  (Enrico Grazi, Dept. of Biochemistry and Molecular Biology, Ferrara, Italy)
Abstract:
A very impressive property of actin is the versatility in the formation of
supramolecular structures. G-actin is converted into filamentous or globular structures, it
is ordered into paracrystalline arrays or in tubular structures. The formation of these
almost regular structures is accompanied by distinct changes of the osmotic properties of
the actin solution so that, in some cases, the geometric parameters of the supramolecular
structure can be related, albeit indirectly, to protein osmotic pressure. With the increase
of protein osmotic pressure protein-bound water is removed and the volume of the system
decreases. These events are necessarily linked to changes of the geometric parameters of
the supramolecular structure. The study of protein osmotic pressure may thus provide
information on the geometry of the supramolecular assembly, even though the geometry
depends in a complex manner on the concentration and charge of the protein. In addition,
change of protein osmotic pressure may signal the transition of the actin filaments into a
network of filaments. The study of osmotic protein pressure allows to determine the
activity and the change of the free energy of the solute in binary solutions and, in some
cases, in ternary solutions. Two further points deserve consideration: A. The free energy
of the free actin monomers is related to the protein osmotic pressure generated by
polymeric actin solutions. B. With the model of Biron et al. [Europhys. Lett 2006, 73,
464] it is possible to relate the change of the free energy of the free actin monomers to the
change of the length distribution of the actin filaments. It follows that the length
distribution of the actin filaments is regulated by (1) the free energy of hydrolysis of ATP
and (2) the protein osmotic pressure. 


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Osmotic Pressure: A Tool to Investigate the Polymeric Forms of Actin pp. 97-136