We studied polymers of desmin, a muscle-specific type ill intermediate fila
ment protein, using quasi-elastic light scattering. Desmin was purified fro
m chicken gizzard. Polymerization was induced either by 2 mM MgCl2 or 150 m
M NaCl. The polymer solutions were in the semidilute regime. We concluded t
hat the persistence length of the filaments is between 0.1 and 1 mu m. In a
ll cases, we found a hydrodynamic diameter of desmin filaments of 16-18 nm.
The filament dynamics exhibits a characteristic frequency in the sense tha
t correlation functions measured on one sample but at different scattering
vectors collapse onto a single master curve when time is normalized by the
experimentally determined initial decay rate.