17 June 1993 Aggregation state of vimentin intermediate filament proteins probed with electric-field-induced birefringence
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Proceedings Volume 1922, Laser Study of Macroscopic Biosystems; (1993) https://doi.org/10.1117/12.146180
Event: Laser Spectroscopy of Biomolecules: 4th International Conference on Laser Applications in Life Sciences, 1992, Jyvaskyla, Finland
Abstract
The structure of the tetrameric building block of vimentin intermediate filaments is determined by transient electric birefringence measurements. The decay time of birefringence, which is determined by hydrodynamic properties of the molecules, was found to be 4.4 +/- 0.5 microsecond(s) at 20 degree(s)C. This corresponds to a 62 - 67 nm long particle, assuming rigid rod- like proteins. This is in agreement with a staggered conformation of two approximately 45 nm long vimentin dimers. An in-register association of two dimers, resulting in an approximately 45 nm long tetramer, is not found.
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Martin Kooijman, Michael Bloemendal, Peter Traub, Herbert van Amerogen, Rienk van Grondelle, "Aggregation state of vimentin intermediate filament proteins probed with electric-field-induced birefringence", Proc. SPIE 1922, Laser Study of Macroscopic Biosystems, (17 June 1993); doi: 10.1117/12.146180; https://doi.org/10.1117/12.146180
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