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. 1999 Oct;77(4):2199–2209. doi: 10.1016/S0006-3495(99)77060-8

Desmin filaments studied by quasi-elastic light scattering.

M Hohenadl 1, T Storz 1, H Kirpal 1, K Kroy 1, R Merkel 1
PMCID: PMC1300500  PMID: 10512839

Abstract

We studied polymers of desmin, a muscle-specific type III intermediate filament protein, using quasi-elastic light scattering. Desmin was purified from chicken gizzard. Polymerization was induced either by 2 mM MgCl(2) or 150 mM NaCl. The polymer solutions were in the semidilute regime. We concluded that the persistence length of the filaments is between 0.1 and 1 microm. In all cases, we found a hydrodynamic diameter of desmin filaments of 16-18 nm. The filament dynamics exhibits a characteristic frequency in the sense that 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.

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Selected References

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