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Proceedings Paper

Aggregation state of vimentin intermediate filament proteins probed with electric-field-induced birefringence
Author(s): Martin Kooijman; Michael Bloemendal; Peter Traub; Herbert van Amerogen; Rienk van Grondelle
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Paper 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.

Paper Details

Date Published: 17 June 1993
PDF: 8 pages
Proc. SPIE 1922, Laser Study of Macroscopic Biosystems, (17 June 1993); doi: 10.1117/12.146180
Show Author Affiliations
Martin Kooijman, Free Univ. (Netherlands)
Michael Bloemendal, Free Univ. (Netherlands)
Peter Traub, Max Planck Institute for Cell Biology (Germany)
Herbert van Amerogen, Free Univ. (Netherlands)
Rienk van Grondelle, Free Univ. (Netherlands)


Published in SPIE Proceedings Vol. 1922:
Laser Study of Macroscopic Biosystems

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